Antimicrobial Plant Peptides: Structure, Classification, Mechanism and Therapeutic Potential

References

1. IshaqN. BilalM. IqbalH.M.N. Medicinal potentialities of plant defensins: A review with applied perspectives.Medicines2019612910.3390/medicines6010029 30791451
   [Google Scholar]
2. YangX. LiJ. LiX. SheR. PeiY. Isolation and characterization of a novel thermostable non-specific lipid transfer protein-like antimicrobial protein from motherwort (Leonurus japonicus Houtt) seeds.Peptides200627123122312810.1016/j.peptides.2006.07.019 16979797
   [Google Scholar]
3. CamposD.C.O. CostaA.S. LuzP.B. SoaresP.M.G. AlencarN.M.N. OliveiraH.D. Morinda citrifolia lipid transfer protein 1 exhibits anti-inflammatory activity by modulation of pro- and anti-inflammatory cytokines.Int. J. Biol. Macromol.20171031121112910.1016/j.ijbiomac.2017.05.148 28559184
   [Google Scholar]
4. AlbersheimP. ValentB.S. Host-pathogen interactions in plants. Plants, when exposed to oligosaccharides of fungal origin, defend themselves by accumulating antibiotics.J. Cell Biol.197878362764310.1083/jcb.78.3.627 359568
   [Google Scholar]
5. VanceC.P. KirkT.K. SherwoodR.T. Lignification as a mechanism of disease resistance.Annual Rev. Phytopathol.198118259288
   [Google Scholar]
6. AistJ.R. Papillae and related wound plugs of plant cells.Annu. Rev. Phytopathol.197614114516310.1146/annurev.py.14.090176.001045
   [Google Scholar]
7. HammerschmidtR. NucklesE.M. KućJ. Association of enhanced peroxidase activity with induced systemic resistance of cucumber to Colletotrichum lagenarium.Physiol. Plant Pathol.1982201738210.1016/0048‑4059(82)90025‑X
   [Google Scholar]
8. ManiS. BhattS.B. VasudevanV. PrabhuD. RajamanikandanS. VelusamyP. RamasamyP. RamanP. The updated review on plant peptides and their applications in human health.Int. J. Pept. Res. Ther.202228513510.1007/s10989‑022‑10437‑7 35911180
   [Google Scholar]
9. TavorminaP. ConinckD.B. NikonorovaN. SmetD.I. CammueB.P.A. The plant peptidome: An expanding repertoire of structural features and biological functions.Plant Cell20152782095211810.1105/tpc.15.00440 26276833
   [Google Scholar]
10. KaurK. DattajiraoV. ShrivastavaV. BhardwajU. Isolation and characterization of chitosan-producing bacteria from beaches of chennai, India.Enzyme Res.201220121610.1155/2012/421683 22919468
    [Google Scholar]
11. HernandezJ.F. GagnonJ. ChicheL. NguyenT.M. AndrieuJ.P. HeitzA. HongT.T. PhamT.T.C. NguyenL.D. Squash trypsin inhibitors from Momordica cochinchinensis exhibit an atypical macrocyclic structure.Biochemistry200039195722573010.1021/bi9929756 10801322
    [Google Scholar]
12. YadavS. BatraJ. Mechanism of Anti-HIV activity of ribosome inactivating protein, saporin.Protein Pept. Lett.201522649750310.2174/0929866522666150428120701 25925771
    [Google Scholar]
13. NaiderF. AnglisterJ. Peptides in the treatment of AIDS.Curr. Opin. Struct. Biol.200919447348210.1016/j.sbi.2009.07.003 19632107
    [Google Scholar]
14. KinghornA.D. ChaiH-B. KinghornA.D. Discovery of new anticancer agents from higher plants.Front. Biosci.2012S4114215610.2741/s257 22202049
    [Google Scholar]
15. GirishK.S. MachiahK.D. UshanandiniS. KumarH.K. NagarajuS. GovindappaM. VedavathiM. KemparajuK. Antimicrobial properties of a non‐toxic glycoprotein (WSG) from Withania somnifera (Ashwagandha).J. Basic Microbiol.200646536537410.1002/jobm.200510108 17009292
    [Google Scholar]
16. ParkJ.S. HwangD.J. LeeS.M. KimY.T. ChoiS.B. ChoK.J. Ribosome-inactivating activity and cDNA cloning of antiviral protein isoforms of Chenopodium album.Mol. Cells2004171738010.1016/S1016‑8478(23)13009‑3 15055531
    [Google Scholar]
17. WalshM.J. DoddJ.E. HautbergueG.M. Ribosome-inactivating proteins.Virulence20134877478410.4161/viru.26399 24071927
    [Google Scholar]
18. HuangL.S. HuangP.L. KungH.F. LiB.Q. HuangP.L. HuangP. HuangH.I. ChenH.C. TAP 29: An anti-human immunodeficiency virus protein from Trichosanthes kirilowii that is nontoxic to intact cells.Proc. Natl. Acad. Sci.199188156570657410.1073/pnas.88.15.6570 1713684
    [Google Scholar]
19. LeaderB. BacaQ.J. GolanD.E. Protein therapeutics: A summary and pharmacological classification.Nat. Rev. Drug Discov.200871213910.1038/nrd2399 18097458
    [Google Scholar]
20. LiuY. LuoJ. XuC. RenF. PengC. WuG. ZhaoJ. Purification, characterization, and molecular cloning of the gene of a seed-specific antimicrobial protein from pokeweed.Plant Physiol.200012241015102410.1104/pp.122.4.1015 10759497
    [Google Scholar]
21. MazalovskaM. KouokamJ.C. Lectins as promising therapeutics for the prevention and treatment of HIV and other potential coinfections.BioMed Res. Int.2018201811210.1155/2018/3750646 29854749
    [Google Scholar]
22. IrvinJ.D. UckunF.M. Pokeweed antiviral protein: Ribosome inactivation and therapeutic applications.Pharmacol. Ther.199255327930210.1016/0163‑7258(92)90053‑3 1492120
    [Google Scholar]
23. WangG. Natural antimicrobial peptides as promising anti-HIV candidates.Curr. Top. Pept. Protein Res.20121393110 26834391
    [Google Scholar]
24. BarbieriL. AronG.M. IrvinJ.D. StirpeF. Purification and partial characterization of another form of the antiviral protein from the seeds of Phytolacca americana L. (pokeweed).Biochem. J.19822031555910.1042/bj2030055 7103950
    [Google Scholar]
25. PelegriniB.P. SartoD.R.P. SilvaO.N. FrancoO.L. Grossi-de-SaM.F. Antibacterial peptides from plants: What they are and how they probably work.Biochem. Res. Int.201120111910.1155/2011/250349 21403856
    [Google Scholar]
26. GerlachS. MondalD. The bountiful biological activities of cyclotides.Chronicl. Young Sci.20123316916910.4103/2229‑5186.99559
    [Google Scholar]
27. ZhouP. YangX-L. WangX-G. HuB. ZhangL. ZhangW. SiH-R. ZhuY. LiB. HuangC-L. A pneumonia outbreak associated with a new coronavirus of probable bat origin.Nature2020579270273
    [Google Scholar]
28. O’KeefeB.R. GiomarelliB. BarnardD.L. ShenoyS.R. ChanP.K.S. McMahonJ.B. PalmerK.E. BarnettB.W. MeyerholzD.K. LenaneW.C.L. McCrayP.B.Jr Broad-spectrum in vitro activity and in vivo efficacy of the antiviral protein griffithsin against emerging viruses of the family Coronaviridae.J. Virol.20108452511252110.1128/JVI.02322‑09 20032190
    [Google Scholar]
29. MilletJ.K. SéronK. LabittR.N. DanneelsA. PalmerK.E. WhittakerG.R. DubuissonJ. BelouzardS. Middle East respiratory syndrome coronavirus infection is inhibited by griffithsin.Antiviral Res.20161331810.1016/j.antiviral.2016.07.011 27424494
    [Google Scholar]
30. LuoZ. SuK. ZhangX. Potential of plant proteins digested in silico by gastrointestinal enzymes as nutritional supplement for COVID-19 patients.Plant Foods Hum. Nutr.202075458359110.1007/s11130‑020‑00850‑y 32870435
    [Google Scholar]
31. DeepthiB. SowjanyaK. LidiyaB. BhargaviR.S. BabuP.S. A modern review of diabetes mellitus: An annihilatory metabolic disorder.J. Sil. Vit. Pharmacol.2017310001410.21767/2469‑6692.100014
    [Google Scholar]
32. LedesmaH.B. HsiehC.C. Chemopreventive role of food-derived proteins and peptides: A review.Crit. Rev. Food Sci. Nutr.201757112358237610.1080/10408398.2015.1057632 26565142
    [Google Scholar]
33. KannanA. HettiarachchyN.S. LayJ.O. LiyanageR. Human cancer cell proliferation inhibition by a pentapeptide isolated and characterized from rice bran.Peptides20103191629163410.1016/j.peptides.2010.05.018 20594954
    [Google Scholar]
34. MatsubayashiY. Post-translational modifications in secreted peptide hormones in plants.Plant Cell Physiol.201152151310.1093/pcp/pcq169 21071428
    [Google Scholar]
35. ParkS. YooK.O. MarcussenT. BacklundA. JacobssonE. RosengrenK.J. DooI. GöranssonU. Cyclotide evolution: Insights from the analyses of their precursor sequences, structures and distribution in violets (Viola).Front. Plant Sci.20178205810.3389/fpls.2017.02058 29326730
    [Google Scholar]
36. ZasloffM. Antimicrobial peptides of multicellular organisms.Nature2002415687038939510.1038/415389a 11807545
    [Google Scholar]
37. MukherjeeS. HooperL.V. Antimicrobial defense of the intestine.Immunity2015421283910.1016/j.immuni.2014.12.028 25607457
    [Google Scholar]
38. TyagiC. MarikT. VágvölgyiC. KredicsL. ÖtvösF. Accelerated molecular dynamics applied to the peptaibol folding problem.Int. J. Mol. Sci.20192017426810.3390/ijms20174268 31480404
    [Google Scholar]
39. TangS.S. ProdhanZ.H. BiswasS.K. LeC.F. SekaranS.D. Antimicrobial peptides from different plant sources: Isolation, characterisation, and purification.Phytochemistry20181549410510.1016/j.phytochem.2018.07.002 30031244
    [Google Scholar]
40. TamJ. WangS. WongK. TanW. Antimicrobial peptides from plants.Pharmaceuticals20158471175710.3390/ph8040711 26580629
    [Google Scholar]
41. KohnE. ShirleyD. ArotskyL. PiccianoA. RidgwayZ. UrbanM. CaroneB. CaputoG. Role of cationic side chains in the antimicrobial activity of C18G.Molecules201823232910.3390/molecules23020329 29401708
    [Google Scholar]
42. CiociolaT. GiovatiL. ContiS. MaglianiW. SantinoliC. PolonelliL. Natural and synthetic peptides with antifungal activity.Future Med. Chem.20168121413143310.4155/fmc‑2016‑0035 27502155
    [Google Scholar]
43. MeloM.N. FerreR. CastanhoM.A.R.B. Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations.Nat. Rev. Microbiol.20097324525010.1038/nrmicro2095 19219054
    [Google Scholar]
44. GroismanE.A. How bacteria resist killing by host-defense peptides.Trends Microbiol.199421144444910.1016/0966‑842X(94)90802‑8 7866702
    [Google Scholar]
45. YaziciA. OrtucuS. TaskinM. MarinelliL. Natural-based antibiofilm and antimicrobial peptides from microorganisms.Curr. Top. Med. Chem.201918242102210710.2174/1568026618666181112143351 30417789
    [Google Scholar]
46. MoyerT.B. HeilL.R. KirkpatrickC.L. GoldfarbD. LefeverW.A. ParsleyN.C. WommackA.J. HicksL.M. PepSAVI-MS reveals a proline-rich antimicrobial peptide in Amaranthus tricolor.J. Nat. Prod.201982102744275310.1021/acs.jnatprod.9b00352 31557021
    [Google Scholar]
47. LeeJ.H. SeoM. LeeH.J. BaekM. KimI.W. KimS.Y. KimM.A. KimS.H. HwangJ.S. Anti-inflammatory activity of antimicrobial peptide allomyrinasin derived from the dynastid beetle, allomyrina dichotoma.J. Microbiol. Biotechnol.2019295687695
    [Google Scholar]
48. KimY.H. KimY.S. ParkC.H. ChungI.Y. YooJ.M. KimJ.G. LeeB.J. KangS.S. ChoG.J. ChoiW.S. Protein kinase C-δ mediates neuronal apoptosis in the retinas of diabetic rats via the Akt signaling pathway.Diabetes20085782181219010.2337/db07‑1431 18443201
    [Google Scholar]
49. LiB. LyuP. XieS. QinH. PuW. XuH. ChenT. ShawC. GeL. KwokH.F. LFB: A novel antimicrobial brevinin-like peptide from the skin secretion of the fujian large headed frog, Limnonectes fujianensi.Biomolecules20199624210.3390/biom9060242 31234333
    [Google Scholar]
50. HoekV.M.L. PrickettM.D. SettlageR.E. KangL. MichalakP. VlietK.A. BishopB.M. The Komodo dragon (Varanus komodoensis) genome and identification of innate immunity genes and clusters.BMC Genomics201920168410.1186/s12864‑019‑6029‑y 31470795
    [Google Scholar]
51. BraunM.S. SporerF. ZimmermannS. WinkM. Birds, feather-degrading bacteria and preen glands: The antimicrobial activity of preen gland secretions from turkeys (Meleagris gallopavo) is amplified by keratinase.FEMS Microbiol. Ecol.2018949fiy11710.1093/femsec/fiy117 29901706
    [Google Scholar]
52. WangA. ChaoT. JiZ. XuanR. LiuS. GuoM. WangG. WangJ. Transcriptome analysis reveals potential immune function-related regulatory genes/pathways of female Lubo goat submandibular glands at different developmental stages.PeerJ20208e994710.7717/peerj.9947 33083113
    [Google Scholar]
53. MattickA.T.R. HirschA. Further observations on an inhibitory substance (Nisin) from lactic streptococci.Lancet19472646258
    [Google Scholar]
54. GharsallaouiA. OulahalN. JolyC. DegraeveP. Nisin as a food preservative: Part 1: Physicochemical properties, antimicrobial activity, and main uses.Crit. Rev. Food Sci. Nutr.20165681262127410.1080/10408398.2013.763765 25675115
    [Google Scholar]
55. ShinJ.M. GwakJ.W. KamarajanP. FennoJ.C. RickardA.H. KapilaY.L. Biomedical applications of nisin.J. Appl. Microbiol.201612061449146510.1111/jam.13033 26678028
    [Google Scholar]
56. KitagawaN. OtaniT. InaiT. Nisin, a food preservative produced by Lactococcus lactis, affects the localization pattern of intermediate filament protein in HaCaT cells.Anat. Sci. Int.201994216317110.1007/s12565‑018‑0462‑x 30353456
    [Google Scholar]
57. AlkotainiB. AnuarN. KadhumA.A.H. SaniA.A.A. Detection of secreted antimicrobial peptides isolated from cell-free culture supernatant of Paenibacillus alvei AN5.J. Ind. Microbiol. Biotechnol.201340657157910.1007/s10295‑013‑1259‑5 23508455
    [Google Scholar]
58. YiT. HuangY. ChenY. Production of an antimicrobial peptide AN5-1 in Escherichia coli and its dual mechanisms against bacteria.Chem. Biol. Drug Des.201585559860710.1111/cbdd.12449 25311453
    [Google Scholar]
59. GutierrezG.E. MayerM.J. CotterP.D. NarbadA. Gut microbiota as a source of novel antimicrobials.Gut Microbes201910112110.1080/19490976.2018.1455790 29584555
    [Google Scholar]
60. PushpanathanP. MathewG.S. SelvarajanS. SeshadriK.G. SrikanthP. Gut microbiota and its mysteries.Indian J. Med. Microbiol.201937226827710.4103/ijmm.IJMM_19_373 31745030
    [Google Scholar]
61. EssigA. HofmannD. MünchD. GayathriS. KünzlerM. KallioP.T. SahlH.G. WiderG. SchneiderT. AebiM. Copsin, a novel peptide-based fungal antibiotic interfering with the peptidoglycan synthesis.J. Biol. Chem.201428950349533496410.1074/jbc.M114.599878 25342741
    [Google Scholar]
62. SrivastavaS. DashoraK. AmetaK.L. SinghN.P. EnshasyE.H.A. PaganoM.C. HeshamA.E.L. SharmaG.D. SharmaM. BhargavaA. Cysteine‐rich antimicrobial peptides from plants: The future of antimicrobial therapy.Phytother. Res.202135125627710.1002/ptr.6823 32940412
    [Google Scholar]
63. TaveiraG.B. MelloÉ.O. SouzaS.B. MonteiroR.M. RamosA.C. CarvalhoA.O. RodriguesR. OkorokovL.A. GomesV.M. Programmed cell death in yeast by thionin-like peptide from Capsicum annuum fruits involving activation of caspases and extracellular H+ flux.Biosci. Rep.2018382BSR2018011910.1042/BSR20180119 29599127
    [Google Scholar]
64. HaoG. BakkerM.G. KimH.S. Enhanced resistance to Fusarium graminearum in transgenic arabidopsis plants expressing a modified plant thionin.Phytopathology202011051056106610.1094/PHYTO‑12‑19‑0447‑R 32043419
    [Google Scholar]
65. LiJ. HuS. JianW. XieC. YangX. Plant antimicrobial peptides: Structures, functions, and applications.Bot. Stud.2021621510.1186/s40529‑021‑00312‑x 33914180
    [Google Scholar]
66. GourbalB. PinaudS. BeckersG.J.M. Van Der MeerJ.W.M. ConrathU. NeteaM.G. Innate immune memory: An evolutionary perspective.Immunol. Rev.20182831214010.1111/imr.12647 29664574
    [Google Scholar]
67. WuQ. PatočkaJ. KučaK. Insect antimicrobial peptides, a mini review.Toxins2018101146110.3390/toxins10110461 30413046
    [Google Scholar]
68. LochG. ZinkeI. MoriT. CarreraP. SchroerJ. TakeyamaH. HochM. Antimicrobial peptides extend lifespan in Drosophila.PLoS One2017125e017668910.1371/journal.pone.0176689 28520752
    [Google Scholar]
69. HansonM.A. LemaitreB. New insights on Drosophila antimicrobial peptide function in host defense and beyond.Curr. Opin. Immunol.202062223010.1016/j.coi.2019.11.008 31835066
    [Google Scholar]
70. ChowdhuryM. LiC.F. HeZ. LuY. LiuX.S. WangY.F. IpY.T. StrandM.R. YuX.Q. Toll family members bind multiple Spätzle proteins and activate antimicrobial peptide gene expression in Drosophila.J. Biol. Chem.201929426101721018110.1074/jbc.RA118.006804 31088910
    [Google Scholar]
71. AgeitosJ.M. PérezS.A. MataC.P. VillaT.G. Antimicrobial peptides (AMPs): Ancient compounds that represent novel weapons in the fight against bacteria.Biochem. Pharmacol.201713311713810.1016/j.bcp.2016.09.018 27663838
    [Google Scholar]
72. MuncasterS. KraakmanK. GibbonsO. MensinkK. ForlenzaM. JacobsonG. BirdS. Antimicrobial peptides within the Yellowtail Kingfish (Seriola lalandi).Dev. Comp. Immunol.201880678010.1016/j.dci.2017.04.014 28433529
    [Google Scholar]
73. AvilaE.E. Functions of antimicrobial peptides in vertebrates.Curr. Protein Pept. Sci.2017181110981119 27526932
    [Google Scholar]
74. HartenV.R.M. WoudenberghV.E. DijkV.A. HaagsmanH.P. Cathelicidins: Immunomodulatory antimicrobials.Vaccines2018636310.3390/vaccines6030063 30223448
    [Google Scholar]
75. ChenC. WangA. ZhangF. ZhangM. YangH. LiJ. SuP. ChenY. YuH. WangY. The protective effect of fish-derived cathelicidins on bacterial infections in zebrafish, Danio rerio.Fish Shellfish Immunol.20199251952710.1016/j.fsi.2019.06.029 31202967
    [Google Scholar]
76. PatockaJ. NepovimovaE. KlimovaB. WuQ. KucaK. Antimicrobial peptides: Amphibian host defense peptides.Curr. Med. Chem.201926325924594610.2174/0929867325666180713125314 30009702
    [Google Scholar]
77. WeiL. YangJ. HeX. MoG. HongJ. YanX. LinD. LaiR. Structure and function of a potent lipopolysaccharide-binding antimicrobial and anti-inflammatory peptide.J. Med. Chem.20135693546355610.1021/jm4004158 23594231
    [Google Scholar]
78. PeinadoP.C. DiasS.A. DominguesM.M. BenfieldA.H. FreireJ.M. BaptistaR.G. GasparD. CastanhoM.A.R.B. CraikD.J. HenriquesS.T. VeigaA.S. AndreuD. Mechanisms of bacterial membrane permeabilization by crotalicidin (Ctn) and its fragment Ctn(15-34), antimicrobial peptides from rattlesnake venom.J. Biol. Chem.201829351536154910.1074/jbc.RA117.000125 29255091
    [Google Scholar]
79. RajasekaranG. KumarS.D. YangS. ShinS.Y. The design of a cell-selective fowlicidin-1-derived peptide with both antimicrobial and anti-inflammatory activities.Eur. J. Med. Chem.201918211162310.1016/j.ejmech.2019.111623 31473417
    [Google Scholar]
80. CoorensM. SchneiderV.A.F. GrootD.A.M. DijkV.A. MeijerinkM. WellsJ.M. ScheenstraM.R. VeldhuizenE.J.A. HaagsmanH.P. Cathelicidins inhibit Escherichia coli -induced TLR2 and TLR4 activation in a viability-dependent manner.J. Immunol.201719941418142810.4049/jimmunol.1602164 28710255
    [Google Scholar]
81. SchneiderV.A.F. CoorensM. OrdonezS.R. BokhovenT.J.L.M. PosthumaG. DijkV.A. HaagsmanH.P. VeldhuizenE.J.A. Imaging the antimicrobial mechanism(s) of cathelicidin-2.Sci. Rep.2016613294810.1038/srep32948 27624595
    [Google Scholar]
82. SpeirsY.M. DrouinD. CavalcanteP.A. BarkemaH.W. CoboE.R. Host defense cathelicidins in cattle: Types, production, bioactive functions and potential therapeutic and diagnostic applications.Int. J. Antimicrob. Agents201851681382110.1016/j.ijantimicag.2018.02.006 29476808
    [Google Scholar]
83. HuynhE. PenneyJ. CaswellJ. LiJ. Protective effects of protegrin in dextran sodium sulfate-induced murine colitis.Front. Pharmacol.20191015610.3389/fphar.2019.00156 30873029
    [Google Scholar]
84. HarmanR.M. YangS. HeM.K. Van de WalleG.R. Antimicrobial peptides secreted by equine mesenchymal stromal cells inhibit the growth of bacteria commonly found in skin wounds.Stem Cell Res. Ther.20178115710.1186/s13287‑017‑0610‑6 28676123
    [Google Scholar]
85. ReczyńskaD. ZalewskaM. CzopowiczM. KabaJ. ZwierzchowskiL. BagnickaE. Small ruminant lentivirus infection influences expression of acute phase proteins and cathelicidin genes in milk somatic cells and peripheral blood leukocytes of dairy goats.Vet. Res.201849111310.1186/s13567‑018‑0607‑x 30424807
    [Google Scholar]
86. PanteleevP.V. BolosovI.A. KalashnikovA.À. KokryakovV.N. ShamovaO.V. EmelianovaA.A. BalandinS.V. OvchinnikovaT.V. Combined antibacterial effects of goat cathelicidins with different mechanisms of action.Front. Microbiol.20189298310.3389/fmicb.2018.02983 30555455
    [Google Scholar]
87. TeddeV. BronzoV. PuggioniG.M.G. PolleraC. CasulaA. CuroneG. MoroniP. UzzauS. AddisM.F. Milk cathelicidin and somatic cell counts in dairy goats along the course of lactation.J. Dairy Res.201986221722110.1017/S0022029919000335 31156071
    [Google Scholar]
88. NakazawaM. MaedaS. OmoriM. KajiK. YokoyamaN. NakagawaT. ChambersJ.K. UchidaK. OhnoK. YonezawaT. MatsukiN. Duodenal expression of antimicrobial peptides in dogs with idiopathic inflammatory bowel disease and intestinal lymphoma.Vet. J.2019249475210.1016/j.tvjl.2019.05.006 31239164
    [Google Scholar]
89. LimaD.M.S.F. SilvaD.R.A. SilvaD.M.F. SilvaD.P.A.B. CostaR.M.P.B. TeixeiraJ.A.C. PortoA.L.F. CavalcantiM.T.H. Brazilian kefir-fermented sheep’s milk, a source of antimicrobial and antioxidant peptides.Probiotics Antimicrob. Proteins201810344645510.1007/s12602‑017‑9365‑8 29285743
    [Google Scholar]
90. PengH. PurkersonJ.M. SchwadererA.L. SchwartzG.J. Metabolic acidosis stimulates the production of the antimicrobial peptide cathelicidin in rabbit urine.Am. J. Physiol. Renal Physiol.20173135F1061F106710.1152/ajprenal.00701.2016 28747361
    [Google Scholar]
91. NagaokaI. TamuraH. ReichJ. Therapeutic potential of cathelicidin peptide LL-37, an antimicrobial agent, in a murine sepsis model.Int. J. Mol. Sci.20202117597310.3390/ijms21175973 32825174
    [Google Scholar]
92. FruitwalaS. NaccacheE.D.W. ChangT.L. Multifaceted immune functions of human defensins and underlying mechanisms.Semin. Cell Dev. Biol.20198816317210.1016/j.semcdb.2018.02.023
    [Google Scholar]
93. PaceB.T. LacknerA.A. PorterE. PaharB. The role of defensins in HIV pathogenesis.Mediators Inflamm.2017201711210.1155/2017/5186904 28839349
    [Google Scholar]
94. ContrerasG. ShirdelI. BraunM.S. WinkM. Defensins: Transcriptional regulation and function beyond antimicrobial activity.Dev. Comp. Immunol.202010410355610.1016/j.dci.2019.103556 31747541
    [Google Scholar]
95. PasupuletiM. SchmidtchenA. MalmstenM. Antimicrobial peptides: Key components of the innate immune system.Crit. Rev. Biotechnol.201232214317110.3109/07388551.2011.594423 22074402
    [Google Scholar]
96. GuraoA. KashyapS.K. SinghR. β-defensins: An innate defense for bovine mastitis.Vet. World201710899099810.14202/vetworld.2017.990‑998 28919695
    [Google Scholar]
97. WangR. MaD. LinL. ZhouC. HanZ. ShaoY. LiaoW. LiuS. Identification and characterization of an avian β-defensin orthologue, avian β-defensin 9, from quails.Appl. Microbiol. Biotechnol.20108741395140510.1007/s00253‑010‑2591‑6 20396878
    [Google Scholar]
98. PeiJ. JiangL. Antimicrobial peptide from mucus of Andrias davidianus: Screening and purification by magnetic cell membrane separation technique.Int. J. Antimicrob. Agents2017501414610.1016/j.ijantimicag.2017.02.013 28461043
    [Google Scholar]
99. ChangY.L. WangZ. IgawaS. ChoiJ.E. WerbelT. NardoD.A. Lipocalin 2: A new antimicrobial in mast cells.Int. J. Mol. Sci.20192010238010.3390/ijms20102380 31091692
    [Google Scholar]
100. SchneiderJ.J. UnholzerA. SchallerM. KortingS.M. KortingH.C. Human defensins.J. Mol. Med.200583858759510.1007/s00109‑005‑0657‑1 15821901
     [Google Scholar]
101. MohammedI. SaidD.G. DuaH.S. Human antimicrobial peptides in ocular surface defense.Prog. Retin. Eye Res.20176112210.1016/j.preteyeres.2017.03.004 28587935
     [Google Scholar]
102. SoaresR.C. PennaC.P.H. MoraesD.V.C.S. VecchiD.R. ClavaudC. BretonL. BrazA.S.K. PaulinoL.C. Dysbiotic bacterial and fungal communities not restricted to clinically affected skin sites in dandruff.Front. Cell. Infect. Microbiol.2016615710.3389/fcimb.2016.00157 27909689
     [Google Scholar]
103. da SilvaP.F. MachadoM.C.C. The dual role of cathelicidins in systemic inflammation.Immunol. Lett.2017182576010.1016/j.imlet.2017.01.004 28082134
     [Google Scholar]
104. VargaJ.F.A. MarinosB.M.P. KatzenbackB.A. Frog skin innate immune defences: Sensing and surviving pathogens.Front. Immunol.20199312810.3389/fimmu.2018.03128 30692997
     [Google Scholar]
105. PeiJ. FengZ. RenT. SunH. HanH. JinW. DangJ. TaoY. Purification, characterization and application of a novel antimicrobial peptide from Andrias davidianus blood.Lett. Appl. Microbiol.2018661384310.1111/lam.12823 29130500
     [Google Scholar]
106. HuiC-Y. GuoY. ZhangW. YangX.Q. GaoC.X. YangX-Y. Isolation and characterization of antimicrobial peptides from healthy male urine.Pak. J. Pharm. Sci.2017302363367 28649057
     [Google Scholar]
107. CorreiaA. WeimannA. Protein antibiotics: Mind your language.Nat. Rev. Microbiol.20211917710.1038/s41579‑020‑00485‑5 33219332
     [Google Scholar]
108. SommaD.A. MorettaA. CanèC. CirilloA. DuilioA. Antimicrobial and antibiofilm peptides.Biomolecules202010465210.3390/biom10040652 32340301
     [Google Scholar]
109. DennisonS.R. HarrisF. MuraM. PhoenixD.A. An atlas of anionic antimicrobial peptides from amphibians.Curr. Protein Pept. Sci.201819882383810.2174/1389203719666180226155035 29484989
     [Google Scholar]
110. AlmarwaniB. PhambuN. HamadaY.Z. MeyaS.A. Interactions of an anionic antimicrobial peptide with Zinc(II): Application to bacterial mimetic membranes.Langmuir20203648145541456210.1021/acs.langmuir.0c02306 33227202
     [Google Scholar]
111. MillerA. WitkiewiczM.A. MikołajczykA. WątłyJ. WilcoxD. WitkowskaD. Rowińska-ŻyrekM. Zn-enhanced Asp-rich antimicrobial peptides: N-Terminal coordination by Zn(II) and Cu(II), which distinguishes Cu(II) binding to different peptides.Int. J. Mol. Sci.20212213697110.3390/ijms22136971 34203496
     [Google Scholar]
112. TeixeiraV. FeioM.J. BastosM. Role of lipids in the interaction of antimicrobial peptides with membranes.Prog. Lipid Res.201251214917710.1016/j.plipres.2011.12.005 22245454
     [Google Scholar]
113. GennaroR. ZanettiM. Structural features and biological activities of the cathelicidin-derived antimicrobial peptides.Biopolymers2000551314910.1002/1097‑0282(2000)55:1<31::AID‑BIP40>3.0.CO;2‑9 10931440
     [Google Scholar]
114. LewiesA. WentzelJ. JacobsG. PlessisD.L. The potential use of natural and structural analogues of antimicrobial peptides in the fight against neglected tropical diseases.Molecules2015208153921543310.3390/molecules200815392 26305243
     [Google Scholar]
115. MookherjeeN. AndersonM.A. HaagsmanH.P. DavidsonD.J. Antimicrobial host defence peptides: Functions and clinical potential.Nat. Rev. Drug Discov.202019531133210.1038/s41573‑019‑0058‑8 32107480
     [Google Scholar]
116. AidoukovitchA. DahlS. FältF. NebelD. SvenssonD. TufvessonE. NilssonB.O. Antimicrobial peptide LL‐37 and its pro‐form, hCAP18, in desquamated epithelial cells of human whole saliva.Eur. J. Oral Sci.202012811610.1111/eos.12664 31825534
     [Google Scholar]
117. FabisiakA. MurawskaN. FichnaJ. LL-37: Cathelicidin-related antimicrobial peptide with pleiotropic activity.Pharmacol. Rep.201668480280810.1016/j.pharep.2016.03.015 27117377
     [Google Scholar]
118. JohanssonJ. GudmundssonG.H. RottenbergM.E. BerndtK.D. AgerberthB. Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37.J. Biol. Chem.199827363718372410.1074/jbc.273.6.3718 9452503
     [Google Scholar]
119. KoehbachJ. CraikD.J. The vast structural diversity of antimicrobial peptides.Trends Pharmacol. Sci.201940751752810.1016/j.tips.2019.04.012 31230616
     [Google Scholar]
120. ZhaoH. Mode of action of antimicrobial peptides [Academic Dissertation].Helsinki: University of Helsinki2003
     [Google Scholar]
121. MattarE.H. AlmehdarH.A. YacoubH.A. UverskyV.N. RedwanE.M. Antimicrobial potentials and structural disorder of human and animal defensins.Cytokine Growth Factor Rev.2016289511110.1016/j.cytogfr.2015.11.002 26598808
     [Google Scholar]
122. LehrerR.I. LuW. α‐Defensins in human innate immunity.Immunol. Rev.201224518411210.1111/j.1600‑065X.2011.01082.x 22168415
     [Google Scholar]
123. TaiK.P. LeV.V. SelstedM.E. OuelletteA.J. Hydrophobic determinants of α-defensin bactericidal activity.Infect. Immun.20148262195220210.1128/IAI.01414‑13 24614658
     [Google Scholar]
124. KoehbachJ. Structure-activity relationships of insect defensins.Front Chem.201754510.3389/fchem.2017.00045 28748179
     [Google Scholar]
125. GuyotN. MeudalH. TrappS. IochmannS. SilvestreA. JoussetG. LabasV. ReverdiauP. LothK. HervéV. AucagneV. DelmasA.F. GodbertR.S. LandonC. Structure, function, and evolution of Gga -AvBD11, the archetype of the structural avian-double-β-defensin family.Proc. Natl. Acad. Sci.2020117133734510.1073/pnas.1912941117 31871151
     [Google Scholar]
126. SitaramN. Antimicrobial peptides with unusual amino acid compositions and unusual structures.Curr. Med. Chem.200613667969610.2174/092986706776055689 16529559
     [Google Scholar]
127. SelstedM. Theta-defensins: Cyclic antimicrobial peptides produced by binary ligation of truncated α-defensins.Curr. Protein Pept. Sci.20045536537110.2174/1389203043379459 15544531
     [Google Scholar]
128. ConibearA.C. RosengrenK.J. DalyN.L. HenriquesS.T. CraikD.J. The cyclic cystine ladder in θ-defensins is important for structure and stability, but not antibacterial activity.J. Biol. Chem.201328815108301084010.1074/jbc.M113.451047 23430740
     [Google Scholar]
129. HolaniR. ShahC. HajiQ. InglisG.D. UwieraR.R.E. CoboE.R. Proline-arginine rich (PR-39) cathelicidin: Structure, expression and functional implication in intestinal health.Comp. Immunol. Microbiol. Infect. Dis.2016499510110.1016/j.cimid.2016.10.004 27865272
     [Google Scholar]
130. FloresH.J.L. RodriguezM.C. ArellanezG.A. MoralesA.A. AvilaE.E. Effect of recombinant prophenin 2 on the integrity and viability of Trichomonas vaginalis.BioMed Res. Int.201520151810.1155/2015/430436 25815316
     [Google Scholar]
131. SmirnovaM.P. KolodkinN.I. KolobovA.A. AfoninV.G. AfoninaI.V. StefanenkoL.I. Shpen’V.M. ShamovaO.V. KolobovA.A. Indolicidin analogs with broad-spectrum antimicrobial activity and low hemolytic activity.Peptides202013217035610.1016/j.peptides.2020.170356 32593681
     [Google Scholar]
132. KhurshidZ. NajeebS. MaliM. MoinS.F. RazaS.Q. ZohaibS. SefatF. ZafarM.S. Histatin peptides: Pharmacological functions and their applications in dentistry.Saudi Pharm. J.2017251253110.1016/j.jsps.2016.04.027 28223859
     [Google Scholar]
133. StarlingS. A new way out for lysozyme.Nat. Rev. Gastroenterol. Hepatol.2017141056756710.1038/nrgastro.2017.118 28831185
     [Google Scholar]
134. RaglandS.A. CrissA.K. From bacterial killing to immune modulation: Recent insights into the functions of lysozyme.PLoS Pathog.2017139e100651210.1371/journal.ppat.1006512 28934357
     [Google Scholar]
135. ZhangW. SuJ. XuH. YuS. LiuY. ZhangY. SunL. YueY. ZhouX. Dicumarol inhibits PDK1 and targets multiple malignant behaviors of ovarian cancer cells.PLoS One2017126e017967210.1371/journal.pone.0179672 28617852
     [Google Scholar]
136. IbrahimH.R. ThomasU. PellegriniA. A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action.J. Biol. Chem.200127647437674377410.1074/jbc.M106317200 11560930
     [Google Scholar]
137. HarfordC. SarkarB. Amino terminal Cu(II)- and Ni(II)-binding (ATCUN) motif of proteins and peptides: Metal binding, DNA cleavage, and other properties.Acc. Chem. Res.199730312313010.1021/ar9501535
     [Google Scholar]
138. PortelinhaJ. DuayS.S. YuS.I. HeilemannK. LibardoM.D.J. JulianoS.A. KlassenJ.L. BozaA.A.M. Antimicrobial peptides and copper(II) ions: Novel therapeutic opportunities.Chem. Rev.202112142648271210.1021/acs.chemrev.0c00921 33524257
     [Google Scholar]
139. WendeC. KulakN. Fluorophore ATCUN complexes: Combining agent and probe for oxidative DNA cleavage.Chem. Commun.20155162123951239810.1039/C5CC04508H 26143739
     [Google Scholar]
140. HeinrichJ. KönigN.F. SobottkaS. SarkarB. KulakN. Flexible vs. rigid bis(2-benzimidazolyl) ligands in Cu(II) complexes: Impact on redox chemistry and oxidative DNA cleavage activity.J. Inorg. Biochem.201919422323210.1016/j.jinorgbio.2019.01.016 30877897
     [Google Scholar]
141. EnokiT.A. SilvaM.I. LorenzonE.N. CilliE.M. PerezK.R. RiskeK.A. LamyM.T. Antimicrobial peptide K 0 -W 6 -Hya1 induces stable structurally modified lipid domains in anionic membranes.Langmuir20183452014202510.1021/acs.langmuir.7b03408 29284086
     [Google Scholar]
142. LinT.Y. WeibelD.B. Organization and function of anionic phospholipids in bacteria.Appl. Microbiol. Biotechnol.2016100104255426710.1007/s00253‑016‑7468‑x 27026177
     [Google Scholar]
143. VanceJ.E. Phospholipid synthesis and transport in mammalian cells.Traffic201516111810.1111/tra.12230 25243850
     [Google Scholar]
144. FlorekO.B. CliftonL.A. WildeM. ArnoldT. GreenR.J. FrazierR.A. Lipid composition in fungal membrane models: Effect of lipid fluidity.Acta Crystallogr. D Struct. Biol.201874121233124410.1107/S2059798318009440 30605137
     [Google Scholar]
145. RenneM.F. KroonD.A.I.P.M. The role of phospholipid molecular species in determining the physical properties of yeast membranes.FEBS Lett.201859281330134510.1002/1873‑3468.12944 29265372
     [Google Scholar]
146. BaxterA.A. LayF.T. PoonI.K.H. KvansakulM. HulettM.D. Tumor cell membrane-targeting cationic antimicrobial peptides: Novel insights into mechanisms of action and therapeutic prospects.Cell. Mol. Life Sci.201774203809382510.1007/s00018‑017‑2604‑z 28770291
     [Google Scholar]
147. DegrooteG.S. GuérardelY. DelannoyP. Gangliosides: Structures, biosynthesis, analysis, and roles in cancer.ChemBioChem201718131146115410.1002/cbic.201600705 28295942
     [Google Scholar]
148. VicenteC.M. SilvaD.D.A. SartorioP.V. SilvaT.D. SaadS.S. NaderH.B. ForonesN.M. TomaL. Heparan sulfate proteoglycans in human colorectal cancer.Anal. Cell. Pathol.2018201811010.1155/2018/8389595 30027065
     [Google Scholar]
149. MatsuzakiK. MuraseO. FujiiN. MiyajimaK. Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore.Biochemistry199534196521652610.1021/bi00019a033 7538786
     [Google Scholar]
150. MatsuzakiK. MuraseO. FujiiN. MiyajimaK. An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation.Biochemistry19963535113611136810.1021/bi960016v 8784191
     [Google Scholar]
151. OmardienS. DrijfhoutJ.W. VazF.M. WenzelM. HamoenL.W. ZaatS.A.J. BrulS. Bactericidal activity of amphipathic cationic antimicrobial peptides involves altering the membrane fluidity when interacting with the phospholipid bilayer.Biochim. Biophys. Acta Biomembr.20181860112404241510.1016/j.bbamem.2018.06.004 29902419
     [Google Scholar]
152. LohnerK. ProssniggF. Biological activity and structural aspects of PGLa interaction with membrane mimetic systems.Biochim. Biophys. Acta Biomembr.2009178881656166610.1016/j.bbamem.2009.05.012 19481533
     [Google Scholar]
153. LipkinR.B. LazaridisT. Implicit membrane investigation of the stability of antimicrobial peptide β-barrels and arcs.J. Membr. Biol.2015248346948610.1007/s00232‑014‑9759‑4 25430621
     [Google Scholar]
154. OrenZ. ShaiY. Mode of action of linear amphipathic α-helical antimicrobial peptides.Biopolymers199847645146310.1002/(SICI)1097‑0282(1998)47:6<451::AID‑BIP4>3.0.CO;2‑F 10333737
     [Google Scholar]
155. ShenkarevZ.O. BalandinS.V. TrunovK.I. ParamonovA.S. SukhanovS.V. BarsukovL.I. ArsenievA.S. OvchinnikovaT.V. Molecular mechanism of action of β-hairpin antimicrobial peptide arenicin: Oligomeric structure in dodecylphosphocholine micelles and pore formation in planar lipid bilayers.Biochemistry201150286255626510.1021/bi200746t 21627330
     [Google Scholar]
156. LyuY. FitriyantiM. NarsimhanG. Nucleation and growth of pores in 1,2-Dimyristoyl-sn-glycero-3-phosphocholine (DMPC)/cholesterol bilayer by antimicrobial peptides melittin, its mutants and cecropin P1.Colloids Surf. B Biointerfaces201917312112710.1016/j.colsurfb.2018.09.049 30278360
     [Google Scholar]
157. MardirossianM. GrzelaR. GiglioneC. MeinnelT. GennaroR. MergaertP. ScocchiM. The host antimicrobial peptide Bac71-35 binds to bacterial ribosomal proteins and inhibits protein synthesis.Chem. Biol.201421121639164710.1016/j.chembiol.2014.10.009 25455857
     [Google Scholar]
158. MardirossianM. PérébaskineN. BenincasaM. GambatoS. HofmannS. HuterP. MüllerC. HilpertK. InnisC.A. TossiA. WilsonD.N. The dolphin proline-rich antimicrobial peptide Tur1A inhibits protein synthesis by targeting the bacterial ribosome.Cell Chem. Biol.2018255530539.e710.1016/j.chembiol.2018.02.004 29526712
     [Google Scholar]
159. LeC.F. GudimellaR. RazaliR. ManikamR. SekaranS.D. Transcriptome analysis of Streptococcus pneumoniae treated with the designed antimicrobial peptides, DM3.Sci. Rep.2016612682810.1038/srep26828 27225022
     [Google Scholar]
160. KragolG. LovasS. VaradiG. CondieB.A. HoffmannR. OtvosL.Jr The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding.Biochemistry200140103016302610.1021/bi002656a 11258915
     [Google Scholar]
161. LeC.F. FangC.M. SekaranS.D. Intracellular targeting mechanisms by antimicrobial peptides.Antimicrob. Agents Chemother.2017614e02340e1610.1128/AAC.02340‑16 28167546
     [Google Scholar]
162. WrońskaA.K. BoguśM.I. Heat shock proteins (HSP 90, 70, 60, and 27) in Galleria mellonella (Lepidoptera) hemolymph are affected by infection with Conidiobolus coronatus (Entomophthorales).PLoS One2020152e022855610.1371/journal.pone.0228556 32027696
     [Google Scholar]
163. SubbalakshmiC. SitaramN. Mechanism of antimicrobial action of indolicidin.FEMS Microbiol. Lett.19981601919610.1111/j.1574‑6968.1998.tb12896.x 9495018
     [Google Scholar]
164. HeS. ZhangJ. LiN. ZhouS. YueB. ZhangM. A TFPI-1 peptide that induces degradation of bacterial nucleic acids, and inhibits bacterial and viral infection in half-smooth tongue sole, Cynoglossus semilaevis.Fish Shellfish Immunol.20176046647310.1016/j.fsi.2016.11.029 27840169
     [Google Scholar]
165. ShuH. ChenH. WangX. HuY. YunY. ZhongQ. ChenW. ChenW. Antimicrobial activity and proposed action mechanism of 3-carene against Brochothrix thermosphacta and Pseudomonas fluorescens.Molecules20192418324610.3390/molecules24183246 31489899
     [Google Scholar]
166. LutkenhausJ. Regulation of cell division in E. coli.Trends Genet.199061222510.1016/0168‑9525(90)90045‑8 2183414
     [Google Scholar]
167. LiL. SunJ. XiaS. TianX. CheserekM.J. LeG. Mechanism of antifungal activity of antimicrobial peptide APP, a cell-penetrating peptide derivative, against Candida albicans: Intracellular DNA binding and cell cycle arrest.Appl. Microbiol. Biotechnol.201610073245325310.1007/s00253‑015‑7265‑y 26743655
     [Google Scholar]
168. CruzG.F. AraujoD.I. TorresM.D.T. NunezF.C. OliveiraV.X.Jr AmbrosioF.N. LombelloC.B. AlmeidaD.V. SilvaF.D. GarciaW. Photochemically-generated silver chloride nanoparticles stabilized by a peptide inhibitor of cell division and its antimicrobial properties.J. Inorg. Organomet. Polym. Mater.20203072464247410.1007/s10904‑019‑01427‑2
     [Google Scholar]
169. HelmerhorstE.J. TroxlerR.F. OppenheimF.G. The human salivary peptide histatin 5 exerts its antifungal activity through the formation of reactive oxygen species.Proc. Natl. Acad. Sci.20019825146371464210.1073/pnas.141366998 11717389
     [Google Scholar]
170. LoboB.M. MolinaA. SolanoR. Constitutive expression of ETHYLENE‐RESPONSE‐FACTOR1 in Arabidopsis confers resistance to several necrotrophic fungi.Plant J.2002291233210.1046/j.1365‑313x.2002.01191.x 12060224
     [Google Scholar]
171. ZélicourtD.A. LetouseyP. ThoironS. CampionC. SimoneauP. ElmorjaniK. MarionD. SimierP. DelavaultP. Ha-DEF1, a sunflower defensin, induces cell death in Orobanche parasitic plants.Planta2007226359160010.1007/s00425‑007‑0507‑1 17375322
     [Google Scholar]
172. BroekaertW.F. CammueB.P.A. BolleD.M.F.C. ThevissenK. SamblanxD.G.W. OsbornR.W. NielsonK. Antimicrobial peptides from plants.Crit. Rev. Plant Sci.199716329732310.1080/07352689709701952
     [Google Scholar]
173. CaleyaD.R.F. PascualG.B. OlmedoG.F. CarboneroP. Susceptibility of phytopathogenic bacteria to wheat purothionins in vitro.Appl. Microbiol.1972235998100010.1128/am.23.5.998‑1000.1972 5031563
     [Google Scholar]
174. NguyenG.K.T. ZhangS. NguyenN.T.K. NguyenP.Q.T. ChiuM.S. HardjojoA. TamJ.P. Discovery and characterization of novel cyclotides originated from chimeric precursors consisting of albumin-1 chain a and cyclotide domains in the Fabaceae family.J. Biol. Chem.201128627242752428710.1074/jbc.M111.229922 21596752
     [Google Scholar]
175. BrogdenK.A. Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?Nat. Rev. Microbiol.20053323825010.1038/nrmicro1098 15703760
     [Google Scholar]
176. LiY. XiangQ. ZhangQ. HuangY. SuZ. Overview on the recent study of antimicrobial peptides: Origins, functions, relative mechanisms and application.Peptides201237220721510.1016/j.peptides.2012.07.001 22800692
     [Google Scholar]
177. CarvalhoA.O. GomesV.M. Plant defensins—prospects for the biological functions and biotechnological properties.Peptides20093051007102010.1016/j.peptides.2009.01.018 19428780
     [Google Scholar]
178. LayF. AndersonM. Defensins--components of the innate immune system in plants.Curr. Protein Pept. Sci.2005618510110.2174/1389203053027575 15638771
     [Google Scholar]
179. KushmerickC. CastroS.M. CruzS.J. BlochC.Jr BeirãoP.S.L. Functional and structural features of γ‐zeathionins, a new class of sodium channel blockers.FEBS Lett.1998440330230610.1016/S0014‑5793(98)01480‑X 9872391
     [Google Scholar]
180. SpelbrinkR.G. DilmacN. AllenA. SmithT.J. ShahD.M. HockermanG.H. Differential antifungal and calcium channel-blocking activity among structurally related plant defensins.Plant Physiol.200413542055206710.1104/pp.104.040873 15299136
     [Google Scholar]
181. HavengaB. NdlovuT. ClementsT. ReynekeB. WasoM. KhanW. Exploring the antimicrobial resistance profiles of WHO critical priority list bacterial strains.BMC Microbiol.201919130310.1186/s12866‑019‑1687‑0 31870288
     [Google Scholar]
182. CocciP. RoncaratiA. CapriottiM. MosconiG. PalermoF.A. Transcriptional alteration of gene biomarkers in hemocytes of wild Ostrea edulis with molecular evidence of infections with Bonamia spp. and/or Marteilia refringens parasites.Pathogens20209532310.3390/pathogens9050323 32357566
     [Google Scholar]
183. ZahedifardF. LeeH. NoJ.H. SalimiM. SeyedN. AsoodehA. RafatiS. Comparative study of different forms of Jellein antimicrobial peptide on Leishmania parasite.Exp. Parasitol.202020910782310.1016/j.exppara.2019.107823 31862270
     [Google Scholar]
184. HegedüsN. MarxF. Antifungal proteins: More than antimicrobials?Fungal Biol. Rev.201326413214510.1016/j.fbr.2012.07.002 23412850
     [Google Scholar]
185. XiaoS. CuiP. ShiW. ZhangY. Identification of essential oils with activity against stationary phase Staphylococcus aureus.BMC Compl. Med. Ther.20202019910.1186/s12906‑020‑02898‑4 32209108
     [Google Scholar]
186. TaggarR. JangraM. DwivediA. BansalK. PatilP.B. BhattacharyyaM.S. NandanwarH. SahooD.K. Bacteriocin isolated from the natural inhabitant of Allium cepa against Staphylococcus aureus.World J. Microbiol. Biotechnol.20213722010.1007/s11274‑020‑02989‑x 33427970
     [Google Scholar]
187. ParkH.K. HaM.H. ParkS.G. KimM.N. KimB.J. KimW. Characterization of the fungal microbiota (mycobiome) in healthy and dandruff-afflicted human scalps.PLoS One201272e3284710.1371/journal.pone.0032847 22393454
     [Google Scholar]
188. WangD. ChenJ. ZhuJ. MouY. Novel cyclotides from Hedyotis Biflora has potent bactericidal activity against gram-negative bacteria and E. Coli drug resistance.Int. J. Clin. Exp. Med.2016995219526
     [Google Scholar]
189. NoonanJ. WilliamsW. ShanX. Investigation of antimicrobial peptide genes associated with fungus and insect resistance in maize.Int. J. Mol. Sci.2017189193810.3390/ijms18091938 28914754
     [Google Scholar]
190. FaullK.F. HigginsonJ. WaringA.J. JohnsonJ. ToT. WhiteleggeJ.P. StevensR.L. FluhartyC.B. FluhartyA.L. Disulfide connectivity in cerebroside sulfate activator is not necessary for biological activity or α-helical content but is necessary for trypsin resistance and strong ligand binding.Arch. Biochem. Biophys.2000376226627410.1006/abbi.2000.1714 10775412
     [Google Scholar]
191. SohailA.A. GaikwadM. KhadkaP. SaaranenM.J. RuddockL.W. Production of extracellular matrix proteins in the cytoplasm of E. coli: Making giants in tiny factories.Int. J. Mol. Sci.202021368810.3390/ijms21030688 31973001
     [Google Scholar]
192. KhooK.K. NortonR.S. Role of disulfide bonds in peptide and protein conformation. Amino acids, peptides and proteins in organic chemistry: Analysis and function of amino acids and peptidesWiley-VCH Verlag GmbH & Co. KGaA2011395417
     [Google Scholar]
193. XiaoJ. ZhangH. NiuL. WangX. Efficient screening of a novel antimicrobial peptide from Jatropha curcas by cell membrane affinity chromatography.J. Agric. Food Chem.20115941145115110.1021/jf103876b 21268582
     [Google Scholar]
194. PrabhuS. DennisonS.R. MuraM. LeaR.W. SnapeT.J. HarrisF. Cn ‐AMP2 from green coconut water is an anionic anticancer peptide.J. Pept. Sci.2014201290991510.1002/psc.2684 25234689
     [Google Scholar]
195. HammamiR. HamidaB.J. VergotenG. FlissI. PhytAMP: A database dedicated to antimicrobial plant peptides.Nucleic Acids Res.200937DatabaseD963D96810.1093/nar/gkn65518836196
     [Google Scholar]
196. EgorovT.A. OdintsovaT.I. PukhalskyV.A. GrishinE.V. Diversity of wheat anti-microbial peptides.Peptides200526112064207310.1016/j.peptides.2005.03.007 16269343
     [Google Scholar]
197. YiliA. MaksimovV. MaQ-L. GaoY-H. VeshkurovaO. SalikhovS. AisaH.A. Antimicrobial peptides from the plants.J. Pharm. Pharmacol.20142627641
     [Google Scholar]
198. WongJ.H. NgT.B. Gymnin, a potent defensin-like antifungal peptide from the Yunnan bean (Gymnocladus chinensis Baill).Peptides200324796396810.1016/S0196‑9781(03)00192‑X 14499273
     [Google Scholar]
199. NgaiP.H.K. NgT.B. A napin-like polypeptide from dwarf Chinese white cabbage seeds with translation-inhibitory, trypsin-inhibitory, and antibacterial activities.Peptides200425217117610.1016/j.peptides.2003.12.012 15062997
     [Google Scholar]
200. ThommaB. CammueB. ThevissenK. Plant defensins.Planta2002216219320210.1007/s00425‑002‑0902‑6 12447532
     [Google Scholar]
201. AlmeidaL.F.D. PaulaJ.F. AlmeidaR.V.D. WilliamsD.W. HeblingJ. CavalcantiY.W. Efficacy of citronella and cinnamon essential oils on Candida albicans biofilms.Acta Odontol. Scand.201674539339810.3109/00016357.2016.1166261 27098375
     [Google Scholar]
202. ThevissenK. WarneckeD.C. FrançoisI.E.J.A. LeipeltM. HeinzE. OttC. ZähringerU. ThommaB.P.H.J. FerketK.K.A. CammueB.P.A. Defensins from insects and plants interact with fungal glucosylceramides.J. Biol. Chem.200427963900390510.1074/jbc.M311165200 14604982
     [Google Scholar]
203. ParkH.C. KangH.Y. ChunJ.H. KooC.J. CheongH.Y. KimY.C. KimC.M. ChungS.W. KimC.J. YooH.J. KooD.Y. KooC.S. LimO.C. LeeY.S. ChoJ.M. Characterization of a stamen-specific cDNA encoding a novel plant defensin in Chinese cabbage.Plant Mol. Biol.2002501576810.1023/A:1016005231852 12139009
     [Google Scholar]
204. YokoyamaS. KatoK. KobaA. MinamiY. WatanabeK. YagiF. Purification, characterization, and sequencing of antimicrobial peptides, Cy-AMP1, Cy-AMP2, and Cy-AMP3, from the Cycad (Cycas revoluta) seeds.Peptides200829122110211710.1016/j.peptides.2008.08.007 18778743
     [Google Scholar]
205. MoritaH. YunY.S. TakeyaK. ItokawaH. YamadaK. SegetalinsB. Segetalins B, C and D, three new cyclic peptides from Vaccaria segetalis.Tetrahedron199551216003601410.1016/0040‑4020(95)00278‑G
     [Google Scholar]
206. MoritaH. SatoY. KobayashiJ. Cyclosquamosins A - G, cyclic peptides from the seeds of Annona squamosa.Tetrahedron199955247509751810.1016/S0040‑4020(99)00372‑5
     [Google Scholar]
207. MoritaH. YunY.S. TakeyaK. ItokawaH. ShirotaO. Thionation of segetalins A and B, cyclic peptides with estrogen-like activity from seeds of Vaccaria segetalis.Bioorg. Med. Chem.19975363163610.1016/S0968‑0896(97)00001‑1 9113340
     [Google Scholar]
208. CammueB.P. BolleD.M.F. TerrasF.R. ProostP. DammeV.J. ReesS.B. VanderleydenJ. BroekaertW.F. Isolation and characterization of a novel class of plant antimicrobial peptides form Mirabilis jalapa L. seeds.J. Biol. Chem.199226742228223310.1016/S0021‑9258(18)45866‑8 1733929
     [Google Scholar]
209. CammueB. ThevissenK. HendriksM. EggermontK. GoderisI.J. ProostP. DammeV.J. OsbornR.W. GuerbetteF. KaderJ.C. BroekaertW.F. A potent antimicrobial protein from onion seeds showing sequence homology to plant lipid transfer proteins.Plant Physiol.1995109244545510.1104/pp.109.2.445 7480341
     [Google Scholar]
210. ParkC.J. ParkC.B. HongS.S. LeeH.S. LeeS.Y. KimS.C. Characterization and cDNA cloning of two glycine- and histidine-rich antimicrobial peptides from the roots of shepherd’s purse, Capsella bursa-pastoris.Plant Mol. Biol.200044218719710.1023/A:1006431320677 11117262
     [Google Scholar]
211. TailorR.H. AclandD.P. AttenboroughS. CammueB.P.A. EvansI.J. OsbornR.W. RayJ.A. ReesS.B. BroekaertW.F. A novel family of small cysteine-rich antimicrobial peptides from seed of Impatiens balsamina is derived from a single precursor protein.J. Biol. Chem.199727239244802448710.1074/jbc.272.39.24480 9305910
     [Google Scholar]
212. ThevissenK. FrançoisI.E.J.A. SijtsmaL. AmerongenA. SchaaperW.M.M. MeloenR. TrumpieP.T. BroekaertW.F. CammueB.P.A. Antifungal activity of synthetic peptides derived from Impatiens balsamina antimicrobial peptides Ib-AMP1 and Ib-AMP4.Peptides20052671113111910.1016/j.peptides.2005.01.008 15949628
     [Google Scholar]
213. WangP. BangJ.K. KimH.J. KimJ.K. KimY. ShinS.Y. Antimicrobial specificity and mechanism of action of disulfide-removed linear analogs of the plant-derived Cys-rich antimicrobial peptide Ib-AMP1.Peptides200930122144214910.1016/j.peptides.2009.09.020 19778562
     [Google Scholar]
214. CastroM. FontesW. Plant defense and antimicrobial peptides.Protein Pept. Lett.2005121111610.2174/0929866053405832 15638798
     [Google Scholar]
215. ShaoF. HuZ. XiongY.M. HuangQ.Z. WangC.G. ZhuR.H. WangD.C. A new antifungal peptide from the seeds of Phytolacca americana: Characterization, amino acid sequence and cDNA cloning.Biochim. Biophys. Acta Protein Struct. Mol. Enzymol.19991430226226810.1016/S0167‑4838(99)00013‑8 10082954
     [Google Scholar]
216. LercheM.H. KragelundB.B. BechL.M. PoulsenF.M. Barley lipid-transfer protein complexed with palmitoyl CoA: The structure reveals a hydrophobic binding site that can expand to fit both large and small lipid-like ligands.Structure19975229130610.1016/S0969‑2126(97)00186‑X 9032083
     [Google Scholar]
217. SeguraA. MorenoM. MadueñoF. MolinaA. OlmedoG.F. Snakin-1, a peptide from potato that is active against plant pathogens.Mol. Plant Microbe Interact.1999121162310.1094/MPMI.1999.12.1.16 9885189
     [Google Scholar]
218. LipkinA. AnisimovaV. NikonorovaA. BabakovA. KrauseE. BienertM. GrishinE. EgorovT. An antimicrobial peptide Ar-AMP from amaranth (Amaranthus retroflexus L.) seeds.Phytochemistry200566202426243110.1016/j.phytochem.2005.07.015 16126239
     [Google Scholar]
219. van der WeerdenN.L. BleackleyM.R. AndersonM.A. Properties and mechanisms of action of naturally occurring antifungal peptides.Cell. Mol. Life Sci.201370193545357010.1007/s00018‑013‑1260‑1 23381653
     [Google Scholar]
220. KooJ.C. LeeS.Y. ChunH.J. CheongY.H. ChoiJ.S. KawabataS. MiyagiM. TsunasawaS. HaK.S. BaeD.W. HanC. LeeB.L. ChoM.J. Two hevein homologs isolated from the seed of Pharbitis nil L. exhibit potent antifungal activity.Biochim. Biophys. Acta Protein Struct. Mol. Enzymol.199813821809010.1016/S0167‑4838(97)00148‑9 9507071
     [Google Scholar]
221. ÁngelesL.H. CisnerosS.E. ZárateL.L. GómezV.E. MezaL.J.E. ZarzosaO.A. Thionin Thi2.1 from Arabidopsis thaliana expressed in endothelial cells shows antibacterial, antifungal and cytotoxic activity.Biotechnol. Lett.200830101713171910.1007/s10529‑008‑9756‑8 18563581
     [Google Scholar]
222. BernhardR.A. MarrA.G. The oxidation of terpenes. I. Mechanism and reaction products of D‐limonene autoxidation.J. Food Sci.196025451753010.1111/j.1365‑2621.1960.tb00363.x
     [Google Scholar]
223. KoikeM. OkamotoT. TsudaS. ImaiR. A novel plant defensin-like gene of winter wheat is specifically induced during cold acclimation.Biochem. Biophys. Res. Commun.20022981465310.1016/S0006‑291X(02)02391‑4 12379218
     [Google Scholar]
224. MirouzeM. SelsJ. RichardO. CzernicP. LoubetS. JacquierA. FrançoisI.E.J.A. CammueB.P.A. LebrunM. BerthomieuP. MarquèsL. A putative novel role for plant defensins: A defensin from the zinc hyper‐accumulating plant, Arabidopsis halleri, confers zinc tolerance.Plant J.200647332934210.1111/j.1365‑313X.2006.02788.x 16792695
     [Google Scholar]
225. KongJ.L. DuX.B. FanC.X. XuJ.F. ZhengX.J. Determination of primary structure of a novel peptide from mistletoe and its antitumor activity.Yao Xue Xue Bao20043910813817 15700822
     [Google Scholar]
226. LiS.S. GullboJ. LindholmP. LarssonR. ThunbergE. SamuelssonG. BohlinL. ClaesonP. Ligatoxin B, a new cytotoxic protein with a novel helix-turn-helix DNA-binding domain from the mistletoe Phoradendron liga.Biochem. J.2002366240541310.1042/bj20020221 12049612
     [Google Scholar]
227. NahirñakV. AlmasiaN.I. FernandezP.V. HoppH.E. EstevezJ.M. CarrariF. RovereV.C. Potato snakin-1 gene silencing affects cell division, primary metabolism, and cell wall composition.Plant Physiol.2012158125226310.1104/pp.111.186544 22080603
     [Google Scholar]
228. LinP. WongJ.H. NgT.B. A defensin with highly potent antipathogenic activities from the seeds of purple pole bean.Biosci. Rep.201030210110910.1042/BSR20090004 19335335
     [Google Scholar]
229. IrelandD.C. ColgraveM.L. CraikD.J. A novel suite of cyclotides from Viola odorata: Sequence variation and the implications for structure, function and stability.Biochem. J.2006400111210.1042/BJ20060627 16872274
     [Google Scholar]
230. HerrmannA. SvangårdE. ClaesonP. GullboJ. BohlinL. GöranssonU. Key role of glutamic acid for the cytotoxic activity of the cyclotide cycloviolacin O2.Cell. Mol. Life Sci.200663223524510.1007/s00018‑005‑5486‑4 16389447
     [Google Scholar]
231. WangS.Y. WuJ.H. NgT.B. YeX.Y. RaoP.F. A non-specific lipid transfer protein with antifungal and antibacterial activities from the mung bean.Peptides20042581235124210.1016/j.peptides.2004.06.004 15350690
     [Google Scholar]
232. DalyN.L. CraikD.J. Bioactive cystine knot proteins.Curr. Opin. Chem. Biol.201115336236810.1016/j.cbpa.2011.02.008 21362584
     [Google Scholar]
233. TamJ.P. LuY.A. YangJ.L. ChiuK.W. An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides.Proc. Natl. Acad. Sci.199996168913891810.1073/pnas.96.16.8913 10430870
     [Google Scholar]
234. WitherupK.M. BoguskyM.J. AndersonP.S. RamjitH. RansomR.W. WoodT. SardanaM. Cyclopsychotride A, a biologically active, 31-residue cyclic peptide isolated from Psychotria longipes.J. Nat. Prod.199457121619162510.1021/np50114a002 7714530
     [Google Scholar]
235. JenningsC.V. RosengrenK.J. DalyN.L. PlanM. StevensJ. ScanlonM.J. WaineC. NormanD.G. AndersonM.A. CraikD.J. Isolation, solution structure, and insecticidal activity of kalata B2, a circular protein with a twist: Do Möbius strips exist in nature?Biochemistry200544385186010.1021/bi047837h 15654741
     [Google Scholar]
236. SouzaD.M.W.R. Desafio de plantas transgênicas de laranja hamlin (Citrus Sinensis L. Osbeck) superexpressando os genes CDR-1 Ou PDF2. 2 Ou GLT1 à infecção com xanthomonas citri subsp. Citri ou candidatus liberibacter asiaticus.PhD Thesis, Universidade de São Paulo2023
     [Google Scholar]
237. FrancoO.L. MuradA.M. LeiteJ.R. MendesP.A.M. PratesM.V. BlochC.Jr Identification of a cowpea γ‐thionin with bactericidal activity.FEBS J.2006273153489349710.1111/j.1742‑4658.2006.05349.x 16824043
     [Google Scholar]
238. ZhangY. LewisK. Fabatins: New antimicrobial plant peptides.FEMS Microbiol. Lett.19971491596410.1111/j.1574‑6968.1997.tb10308.x 9103978
     [Google Scholar]
239. FujimuraM. IdeguchiM. MinamiY. WatanabeK. TaderaK. Amino acid sequence and antimicrobial activity of chitin-binding peptides, Pp-AMP 1 and Pp-AMP 2, from Japanese bamboo shoots (Phyllostachys pubescens).Biosci. Biotechnol. Biochem.200569364264510.1271/bbb.69.642 15784998
     [Google Scholar]
240. VernonL.P. EvettG.E. ZeikusR.D. GrayW.R. A toxic thionin from Pyrularia pubera: Purification, properties, and amino acid sequence.Arch. Biochem. Biophys.19852381182910.1016/0003‑9861(85)90136‑5 3985614
     [Google Scholar]
241. BlochC.Jr RichardsonM. A new family of small (5 kDa) protein inhibitors of insect α‐amylases from seeds or sorghum (Sorghum bicolor (L) Moench) have sequence homologies with wheat γ‐purothionins.FEBS Lett.1991279110110410.1016/0014‑5793(91)80261‑Z 1995329
     [Google Scholar]
242. MorenoM. SeguraA. OlmedoG.F. Pseudothionin‐St1, a potato peptide active against potato pathogens.Eur. J. Biochem.1994223113513910.1111/j.1432‑1033.1994.tb18974.x 8033886
     [Google Scholar]
243. SeguraA. MorenoM. MolinaA. OlmedoG.F. Novel defensin subfamily from spinach (Spinacia oleracea).FEBS Lett.19984352-315916210.1016/S0014‑5793(98)01060‑6 9762899
     [Google Scholar]
244. ZottichU. CunhaD.M. CarvalhoA.O. DiasG.B. SilvaN.C.M. SantosI.S. NacimentoD.V.V. MiguelE.C. MachadoO.L.T. GomesV.M. Purification, biochemical characterization and antifungal activity of a new lipid transfer protein (LTP) from Coffea canephora seeds with α-amylase inhibitor properties.Biochim. Biophys. Acta, Gen. Subj.20111810437538310.1016/j.bbagen.2010.12.002 21167915
     [Google Scholar]
245. MuradA.M. PelegriniP.B. NetoS.M. FrancoO.L. Novel findings of defensins and their utilization in construction of transgenic plants.Transgenic Plant J.200713948
     [Google Scholar]
246. WongJ.H. ZhangX.Q. WangH.X. NgT.B. A mitogenic defensin from white cloud beans (Phaseolus vulgaris).Peptides20062792075208110.1016/j.peptides.2006.03.020 16687191
     [Google Scholar]
247. ZuY. YuH. LiangL. FuY. EfferthT. LiuX. WuN. Activities of ten essential oils towards Propionibacterium acnes and PC-3, A-549 and MCF-7 cancer cells.Molecules20101553200321010.3390/molecules15053200 20657472
     [Google Scholar]
248. MaD.Z. WangH.X. NgT.B. A peptide with potent antifungal and antiproliferative activities from Nepalese large red beans.Peptides200930122089209410.1016/j.peptides.2009.08.017 19720103
     [Google Scholar]
249. YountN.Y. YeamanM.R. Multidimensional signatures in antimicrobial peptides.Proc. Natl. Acad. Sci.2004101197363736810.1073/pnas.0401567101 15118082
     [Google Scholar]
250. WongJ.H. NgT.B. Lunatusin, a trypsin-stable antimicrobial peptide from lima beans (Phaseolus lunatus L.).Peptides200526112086209210.1016/j.peptides.2005.03.004 16269344
     [Google Scholar]
251. OrtanA. CampeanuG.H. PirvuD.C. PopescuL. Studies concerning the entrapment of anethum graveolens essential oil in liposomes.Rom. Biotechnol. Lett.20091444114417
     [Google Scholar]
252. PortoW.F. FrancoO.L. Theoretical structural insights into the snakin/GASA family.Peptides20134416316710.1016/j.peptides.2013.03.014 23578978
     [Google Scholar]
253. MartinsJ.C. MaesD. LorisR. PepermansH.A.M. WynsL. WillemR. VerheydenP. H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.J. Mol. Biol.1996258232233310.1006/jmbi.1996.0253 8627629
     [Google Scholar]
254. FujimuraM. MinamiY. WatanabeK. TaderaK. Purification, characterization, and sequencing of a novel type of antimicrobial peptides, Fa-AMP1 and Fa-AMP2, from seeds of buckwheat (Fagopyrum esculentum Moench.).Biosci. Biotechnol. Biochem.20036781636164210.1271/bbb.67.1636 12951494
     [Google Scholar]
255. VerheydenP. PletinckxJ. MaesD. PepermansH.A.M. WynsL. WillemR. MartinsJ. 1 H NMR study of the interaction of N, N ′, N ″‐triacetyl chitotriose with Ac‐AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.FEBS Lett.1995370324524910.1016/0014‑5793(95)00835‑W 7656986
     [Google Scholar]
256. Van den BerghK.P.B. RougéP. ProostP. CoosemansJ. KrouglovaT. EngelborghsY. PeumansW.J. DammeV.E.J.M. Synergistic antifungal activity of two chitin-binding proteins from spindle tree (Euonymus europaeus L.).Planta2004219222123210.1007/s00425‑004‑1238‑1 15048569
     [Google Scholar]
257. GoyalR.K. MattooA.K. Plant antimicrobial peptides.Host defense peptides and their potential as therapeutic agents. EpandR.M. ChamSpringer International Publishing201611113610.1007/978‑3‑319‑32949‑9_5
     [Google Scholar]
258. WeinholdA. DorchehK.E. LiR. RameshkumarN. BaldwinI.T. Antimicrobial peptide expression in a wild tobacco plant reveals the limits of host-microbe-manipulations in the field.eLife20187e2871510.7554/eLife.28715 29661271
     [Google Scholar]
259. MarcusJ.P. GreenJ.L. GoulterK.C. MannersJ.M. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels.Plant J.199919669971010.1046/j.1365‑313x.1999.00569.x 10571855
     [Google Scholar]
260. FantF. VrankenW.F. BorremansF.A.M. The three-dimensional solution structure ofAesculus hippocastanum antimicrobial protein 1 determined by1H nuclear magnetic resonance.Proteins199937338840310.1002/(SICI)1097‑0134(19991115)37:3<388::AID‑PROT7>3.0.CO;2‑F 10591099
     [Google Scholar]
261. WangH.X. NgT.B. Dendrocin, a distinctive antifungal protein from bamboo shoots.Biochem. Biophys. Res. Commun.2003307375075510.1016/S0006‑291X(03)01229‑4 12893287
     [Google Scholar]
262. WangH. NgT.B. Ginkbilobin, a novel antifungal protein from Ginkgo biloba seeds with sequence similarity to embryo-abundant protein.Biochem. Biophys. Res. Commun.2000279240741110.1006/bbrc.2000.3929 11118300
     [Google Scholar]
263. LopezJ. TaitS.W.G. Mitochondrial apoptosis: Killing cancer using the enemy within.Br. J. Cancer2015112695796210.1038/bjc.2015.85 25742467
     [Google Scholar]
264. KerengaB.K. McKennaJ.A. HarveyP.J. QuimbarP. CeronG.D. LayF.T. PhanT.K. VeneerP.K. VasaS. ParisiK. ShafeeT.M.A. van der WeerdenN.L. HulettM.D. CraikD.J. AndersonM.A. BleackleyM.R. Salt-tolerant antifungal and antibacterial activities of the corn defensin ZmD32.Front. Microbiol.20191079510.3389/fmicb.2019.00795 31031739
     [Google Scholar]
265. TavaresL. NoreñaC.P.Z. Encapsulation of ginger essential oil using complex coacervation method: Coacervate formation, rheological property, and physicochemical characterization.Food Bioprocess Technol.20201381405142010.1007/s11947‑020‑02480‑3
     [Google Scholar]
266. TikotskaiaK.M. Investigation of the vitamin P activity of a soluble preparation of rutin.Biull. Eksp. Biol. Med.19584543235 13535899
     [Google Scholar]
267. LayF.T. BruglieraF. AndersonM.A. Isolation and properties of floral defensins from ornamental tobacco and petunia.Plant Physiol.200313131283129310.1104/pp.102.016626 12644678
     [Google Scholar]
268. CastagnaroA. MarañaC. CarboneroP. OlmedoG.F. Extreme divergence of a novel wheat thionin generated by a mutational burst specifically affecting the mature protein domain of the precursor.J. Mol. Biol.199222441003100910.1016/0022‑2836(92)90465‑V 1569564
     [Google Scholar]
269. KhanM.S.A. AhmadI. Biofilm inhibition by Cymbopogon citratus and Syzygium aromaticum essential oils in the strains of Candida albicans.J. Ethnopharmacol.2012140241642310.1016/j.jep.2012.01.045 22326355
     [Google Scholar]
270. TerrasF.R.G. GoderisI.J. LeuvenV.F. VanderleydenJ. CammueB.P.A. BroekaertW.F. in vitro antifungal activity of a radish (Raphanus sativus L.) seed protein homologous to nonspecific lipid transfer proteins.Plant Physiol.199210021055105810.1104/pp.100.2.1055 16653017
     [Google Scholar]
271. GaoA.G. HakimiS.M. MittanckC.A. WuY. WoernerB.M. StarkD.M. ShahD.M. LiangJ. RommensC.M.T. Fungal pathogen protection in potato by expression of a plant defensin peptide.Nat. Biotechnol.200018121307131010.1038/82436 11101813
     [Google Scholar]
272. MaitraN. CushmanJ.C. Isolation and characterization of a drought-induced soybean cDNA encoding a D95 family late-embryogenesis-abundant protein.Plant Physiol.1994106280580610.1104/pp.106.2.805 7991700
     [Google Scholar]
273. ZhuS. GaoB. TytgatJ. Phylogenetic distribution, functional epitopes and evolution of the CSαβ superfamily.Cell. Mol. Life Sci.20056219-202257226910.1007/s00018‑005‑5200‑6 16143827
     [Google Scholar]
274. HuangW. VernonL.P. BellJ.D. Enhancement of adenylate cyclase activity in S49 lymphoma cell membranes by the toxin thionin from Pyrularia pubera.Toxicon199432778979710.1016/0041‑0101(94)90004‑3 7940586
     [Google Scholar]
275. HuangR.H. XiangY. LiuX.Z. ZhangY. HuZ. WangD.C. Two novel antifungal peptides distinct with a five‐disulfide motif from the bark of Eucommia ulmoides Oliv.FEBS Lett.20025211-3879010.1016/S0014‑5793(02)02829‑6 12067732
     [Google Scholar]
276. ConinckD.B. CammueB.P.A. ThevissenK. Modes of antifungal action and in planta functions of plant defensins and defensin-like peptides.Fungal Biol. Rev.201326410912010.1016/j.fbr.2012.10.002
     [Google Scholar]
277. WijesundaraN.M. RupasingheH.P.V. Essential oils from Origanum vulgare and Salvia officinalis exhibit antibacterial and anti-biofilm activities against Streptococcus pyogenes.Microb. Pathog.201811711812710.1016/j.micpath.2018.02.026 29452197
     [Google Scholar]
278. KhanS.R. IqbalA. MalakR. ShehryarK. AttiaS. AhmedT. KhanA.M. ArifM. MiiM. Plant defensins: Types, mechanism of action and prospects of genetic engineering for enhanced disease resistance in plants.3 Biotech20199192
     [Google Scholar]
279. ArnoldR.J. DonnellyA. AltieriL. WongK.S. SungJ. Assessment of outcomes and parental effect on Quality-of-Life endpoints in the management of atopic dermatitis.Manag. Care Interface20072021823 17405577
     [Google Scholar]
280. WongC.T.T. TaichiM. NishioH. NishiuchiY. TamJ.P. Optimal oxidative folding of the novel antimicrobial cyclotide from Hedyotis biflora requires high alcohol concentrations.Biochemistry201150337275728310.1021/bi2007004 21776968
     [Google Scholar]
281. LacerdaA.F. VasconcelosÃ.A.R. PelegriniP.B. Grossi de SaM.F. Antifungal defensins and their role in plant defense.Front. Microbiol.2014511610.3389/fmicb.2014.00116 24765086
     [Google Scholar]
282. MichaelsonD. RaynerJ. CoutoM. GanzT. Cationic defensins arise from charge-neutralized propeptides: A mechanism for avoiding leukocyte autocytotoxicity?J. Leukoc. Biol.199251663463910.1002/jlb.51.6.634 1613398
     [Google Scholar]
283. MatasyohJ.C. KiplimoJ.J. KarubiuN.M. HailstorksT.P. Chemical composition and antimicrobial activity of essential oil of Tarchonanthus camphoratus.Food Chem.200710131183118710.1016/j.foodchem.2006.03.021
     [Google Scholar]
284. SilversteinK.A.T. GrahamM.A. PaapeT.D. VandenBoschK.A. Genome organization of more than 300 defensin-like genes in Arabidopsis.Plant Physiol.2005138260061010.1104/pp.105.060079 15955924
     [Google Scholar]
285. KobayashiY. TakashimaH. TamaokiH. KyogokuY. LambertP. KurodaH. ChinoN. WatanabeT.X. KimuraT. SakakibaraS. MoroderL. The cystine‐stabilized α‐helix: A common structural motif of ion‐channel blocking neurotoxic peptides.Biopolymers199131101213122010.1002/bip.360311009 1724185
     [Google Scholar]
286. BontemsF. RoumestandC. GilquinB. MénezA. TomaF. Refined structure of charybdotoxin: Common motifs in scorpion toxins and insect defensins.Science199125450371521152310.1126/science.1720574 1720574
     [Google Scholar]
287. CampsF.J.C. Three-dimensional model of the insect-directed scorption toxin fromAndroctonus australis hector and its implication for the evolution of scorption toxins in general.J. Mol. Evol.1989291636710.1007/BF02106182 2504931
     [Google Scholar]
288. AlmeidaD.M. WethingtonE. KesslerR.C. The daily inventory of stressful events: An interview-based approach for measuring daily stressors.Assessment200291415510.1177/1073191102091006 11911234
     [Google Scholar]
289. JanssenB.J.C. SchirraH.J. LayF.T. AndersonM.A. CraikD.J. Structure of Petunia hybrida defensin 1, a novel plant defensin with five disulfide bonds.Biochemistry200342278214822210.1021/bi034379o 12846570
     [Google Scholar]
290. LandonC. VovelleF. SodanoP. PajonA. The active site of drosomycin, a small insect antifungal protein, delineated by comparison with the modeled structure of Rs ‐AFP2, a plant antifungal protein.J. Pept. Res.200056423123810.1034/j.1399‑3011.2000.00757.x 11083062
     [Google Scholar]
291. LiuY.J. ChengC.S. LaiS.M. HsuM.P. ChenC.S. LyuP.C. Solution structure of the plant defensin VrD1 from mung bean and its possible role in insecticidal activity against bruchids.Proteins200663477778610.1002/prot.20962 16544327
     [Google Scholar]
292. SongX. ZhouZ. WangJ. WuF. GongW. Purification, characterization and preliminary crystallographic studies of a novel plant defensin from Pachyrrhizus erosus seeds.Acta Crystallogr. D Biol. Crystallogr.20046061121112410.1107/S0907444904007395 15159575
     [Google Scholar]
293. SongS. LaipisP.J. BernsK.I. FlotteT.R. Effect Of DNA-dependent protein kinase on the molecular fate of the rAAV2 genome in skeletal muscle.Proc. Natl. Acad. Sci.20019874084408810.1073/pnas.061014598 11274433
     [Google Scholar]
294. NtuiV.O. ThirukkumaranG. AzadiP. KhanR.S. NakamuraI. MiiM. Stable integration and expression of wasabi defensin gene in “Egusi” melon (Colocynthis citrullus L.) confers resistance to Fusarium wilt and Alternaria leaf spot.Plant Cell Rep.201029994395410.1007/s00299‑010‑0880‑2 20552202
     [Google Scholar]
295. KanzakiH. NirasawaS. SaitohH. ItoM. NishiharaM. TerauchiR. NakamuraI. Overexpression of the wasabi defensin gene confers enhanced resistance to blast fungus (Magnaporthe grisea) in transgenic rice.Theor. Appl. Genet.2002105680981410.1007/s00122‑001‑0817‑9 12582903
     [Google Scholar]
296. LinP. XiaL. WongJ.H. NgT.B. YeX. WangS. XiangzhuS. Lipid transfer proteins from Brassica campestris and mung bean surpass mung bean chitinase in exploitability.J. Pept. Sci.2007131064264810.1002/psc.893 17726719
     [Google Scholar]
297. JhaS. ChattooB.B. Expression of a plant defensin in rice confers resistance to fungal phytopathogens.Transgenic Res.201019337338410.1007/s11248‑009‑9315‑7 19690975
     [Google Scholar]
298. TerrasF.R. EggermontK. KovalevaV. RaikhelN.V. OsbornR.W. KesterA. ReesS.B. TorrekensS. LeuvenV.F. VanderleydenJ. Small cysteine-rich antifungal proteins from radish: Their role in host defense.Plant Cell199575573588 7780308
     [Google Scholar]
299. ChoiW.S. YanM. NusinowD. GrallaJ.D. In vitro transcription and start site selection in Schizosaccharomyces pombe.J. Mol. Biol.200231951005101310.1016/S0022‑2836(02)00329‑7 12079343
     [Google Scholar]
300. KazanK. SchenkP.M. WilsonI. MannersJ.M. DNA microarrays: New tools in the analysis of plant defence responses.Mol. Plant Pathol.20012317718510.1046/j.1364‑3703.2001.00061.x 20573005
     [Google Scholar]
301. BraicuC. PileckiV. BalacescuO. IrimieA. NeagoeB.I. The relationships between biological activities and structure of flavan-3-ols.Int. J. Mol. Sci.201112129342935310.3390/ijms12129342 22272136
     [Google Scholar]
302. GasparY.M. McKennaJ.A. McGinnessB.S. HinchJ. PoonS. ConnellyA.A. AndersonM.A. HeathR.L. Field resistance to Fusarium oxysporum and Verticillium dahliae in transgenic cotton expressing the plant defensin NaD1.J. Exp. Bot.20146561541155010.1093/jxb/eru021 24502957
     [Google Scholar]
303. AnuradhaS.T. DivyaK. JamiS.K. KirtiP.B. Transgenic tobacco and peanut plants expressing a mustard defensin show resistance to fungal pathogens.Plant Cell Rep.200827111777178610.1007/s00299‑008‑0596‑8 18758784
     [Google Scholar]
304. BacharachA.L. CoatesM.Ė. MiddletonT.R. A biological test for vitamin P activity.Biochem. J.1942365-640741210.1042/bj0360407b 16747541
     [Google Scholar]
305. RomeroA. AlamilloJ.M. OlmedoG.F. Processing of thionin precursors in barley leaves by a vacuolar proteinase.Eur. J. Biochem.19972431-220220810.1111/j.1432‑1033.1997.0202a.x 9030740
     [Google Scholar]
306. StevensC. TitarenkoE. HargreavesJ.A. GurrS.J. Defence-related gene activation during an incompatible interaction between Stagonospora (Septoria) nodorum and barley (Hordeum vulgare L.) coleoptile cells.Plant Mol. Biol.199631474174910.1007/BF00019462 8806405
     [Google Scholar]
307. ThevissenK. GhaziA. SamblanxD.G.W. BrownleeC. OsbornR.W. BroekaertW.F. Fungal membrane responses induced by plant defensins and thionins.J. Biol. Chem.199627125150181502510.1074/jbc.271.25.15018 8663029
     [Google Scholar]
308. FischerS.G. ApelK. Organ-specific expression of highly divergent thionin variants that are distinct from the seed-specific crambin in the crucifer Crambe abyssinica.Mol. Gen. Genet.1994245338038910.1007/BF00290119 7816048
     [Google Scholar]
309. BallE.D. TinkhamE.R. FlockR. VorhiesC.T. The grasshoppers and other orthoptera of Arizona;The University of Arizona1942
     [Google Scholar]
310. PonzF. AresP.J. LucasH.C. CarboneroP. OlmedoG.F. Synthesis and processing of thionin precursors in developing endosperm from barley (Hordeum vulgare L.).EMBO J.1983271035104010.1002/j.1460‑2075.1983.tb01542.x 16453465
     [Google Scholar]
311. SteinmüllerK. BatschauerA. ApelK. Tissue‐specific and light‐dependent changes of chromatin organization in barley (Hordeum vulgare).Eur. J. Biochem.1986158351952510.1111/j.1432‑1033.1986.tb09785.x 3015615
     [Google Scholar]
312. GausingK. Thionin genes specifically expressed in barley leaves.Planta1987171224124610.1007/BF00391100 24227332
     [Google Scholar]
313. EppleP. ApelK. BohlmannH. An Arabidopsis thaliana thionin gene is inducible via a signal transduction pathway different from that for pathogenesis-related proteins.Plant Physiol.1995109381382010.1104/pp.109.3.813 8552715
     [Google Scholar]
314. BohlmannH. ApelK. Isolation and characterization of cDNAs coding for leaf-specific thionins closely related to the endosperm-specific hordothionin of barley (Hordeum vulgare L.).Mol. Gen. Genet.19872072-344645410.1007/BF00331614
     [Google Scholar]
315. StecB. MarkmanO. RaoU. HeffronG. HendersonS. VernonL.P. BrumfeldV. TeeterM.M. Proposal for molecular mechanism of thionins deduced from physico‐chemical studies of plant toxins.J. Pept. Res.200464621022410.1111/j.1399‑3011.2004.00187.x 15613085
     [Google Scholar]
316. BohlmannH. ApelK. Thionins.Annu. Rev. Plant Physiol. Plant Mol. Biol.199142122724010.1146/annurev.pp.42.060191.001303
     [Google Scholar]
317. VernonL.P. Pyrularia thionin: Physical properties, biological responses and comparison to other thionins and cardiotoxin.J. Toxicol. Toxin Rev.199211316919110.3109/15569549209115819
     [Google Scholar]
318. RodriguezC.M. FreireM.A. CamilleriC. RobagliaC. The Arabidopsis thaliana cDNAs coding for eIF4E and eIF(iso)4E are not functionally equivalent for yeast complementation and are differentially expressed during plant development.Plant J.199813446547310.1046/j.1365‑313X.1998.00047.x 9680993
     [Google Scholar]
319. HughesP. DennisE. WhitecrossM. LlewellynD. GageP. The cytotoxic plant protein, β-purothionin, forms ion channels in lipid membranes.J. Biol. Chem.2000275282382710.1074/jbc.275.2.823 10625613
     [Google Scholar]
320. StecB. Plant thionins - the structural perspective.Cell. Mol. Life Sci.200663121370138510.1007/s00018‑005‑5574‑5 16715411
     [Google Scholar]
321. BurtS.A. ReindersR.D. Antibacterial activity of selected plant essential oils against Escherichia coli O157:H7.Lett. Appl. Microbiol.200336316216710.1046/j.1472‑765X.2003.01285.x 12581376
     [Google Scholar]
322. EvansJ. WangY.D. ShawK.P. VernonL.P. Cellular responses to Pyrularia thionin are mediated by Ca2+ influx and phospholipase A2 activation and are inhibited by thionin tyrosine iodination.Proc. Natl. Acad. Sci.198986155849585310.1073/pnas.86.15.5849 2503825
     [Google Scholar]
323. SchmidtM. ArendtE.K. TheryT.L.C. Isolation and characterisation of the antifungal activity of the cowpea defensin Cp-thionin II.Food Microbiol.20198250451410.1016/j.fm.2019.03.021 31027812
     [Google Scholar]
324. TaveiraG.B. MathiasL.S. MottaD.O.V. MachadoO.L.T. RodriguesR. CarvalhoA.O. FerreiraT.A. PeralesJ. VasconcelosI.M. GomesV.M. Thionin‐like peptides from Capsicum annuum fruits with high activity against human pathogenic bacteria and yeasts.Biopolymers20141021303910.1002/bip.22351 23896704
     [Google Scholar]
325. OardS. KarkiB. EnrightF. Is there a difference in metal ion-based inhibition between members of thionin family: Molecular dynamics simulation study.Biophys. Chem.20071301-2657510.1016/j.bpc.2007.07.005 17703869
     [Google Scholar]
326. OardS.V. Deciphering a mechanism of membrane permeabilization by α-hordothionin peptide.Biochim. Biophys. Acta Biomembr.2011180861737174510.1016/j.bbamem.2011.02.003 21315063
     [Google Scholar]
327. VernonL.P. BellJ.D. Membrane structure, toxins and phospholipase A2 activity.Pharmacol. Ther.199254326929510.1016/0163‑7258(92)90003‑I 1465478
     [Google Scholar]
328. DiazI. CarmonaM.J. OlmedoG.F. Effects of thionins on β‐glucuronidase in vitro and in plant protoplasts.FEBS Lett.1992296327928210.1016/0014‑5793(92)80304‑Y 1537404
     [Google Scholar]
329. WoynarowskiJ.M. KonopaJ. Interaction between DNA and viscotoxins. Cytotoxic basic polypeptides from Viscum album L.Hoppe Seylers Z. Physiol. Chem.198036121535154610.1515/bchm2.1980.361.2.1535 7192684
     [Google Scholar]
330. TabiascoJ. PontF. FourniéJ.J. VercelloneA. Mistletoe viscotoxins increase natural killer cell‐mediated cytotoxicity.Eur. J. Biochem.2002269102591260010.1046/j.1432‑1033.2002.02932.x 12027898
     [Google Scholar]
331. AsanoT. MiwaA. MaedaK. KimuraM. NishiuchiT. The secreted antifungal protein thionin 2.4 in Arabidopsis thaliana suppresses the toxicity of a fungal fruit body lectin from Fusarium graminearum.PLoS Pathog.201398e100358110.1371/journal.ppat.1003581 23990790
     [Google Scholar]
332. OdintsovaT.I. SlezinaM.P. IstominaE.A. KorostylevaT.V. KovtunA.S. KasianovA.S. ShcherbakovaL.A. KudryavtsevA.M. Non-specific lipid transfer proteins in Triticum kiharae Dorof. et Migush.: Identification, characterization and expression profiling in response to pathogens and resistance inducers.Pathogens20198422110.3390/pathogens8040221 31694319
     [Google Scholar]
333. FrackiW.S. LiD. OwenN. PerryC. NaisbittG.H. VernonL.P. Role of Tyr and Trp in membrane responses of Pyrularia thionin determined by optical and NMR spectra following Tyr iodination and Trp modification.Toxicon199230111427144010.1016/0041‑0101(92)90518‑A 1485338
     [Google Scholar]
334. GiudiciM. PovedaA.J. MolinaM.L. de la CanalL. RosG.J.M. PfüllerK. PfüllerU. VillalaínJ. Antifungal effects and mechanism of action of viscotoxin A 3.FEBS J.20062731728310.1111/j.1742‑4658.2005.05042.x 16367749
     [Google Scholar]
335. BüssingA. VerveckenW. WagnerM. WagnerB. PfüllerU. SchietzelM. Expression of mitochondrial Apo2.7 molecules and caspase-3 activation in human lymphocytes treated with the ribosome-inhibiting mistletoe lectins and the cell membrane permeabilizing viscotoxins.Cytometry19993713313910.1002/(SICI)1097‑0320(19991001)37:2<133::AID‑CYTO6>3.0.CO;2‑A 10486525
     [Google Scholar]
336. CoulonA. BerkaneE. SautereauA.M. UrechK. RougéP. LopezA. Modes of membrane interaction of a natural cysteine-rich peptide: Viscotoxin A3.Biochim. Biophys. Acta Biomembr.20021559214515910.1016/S0005‑2736(01)00446‑1 11853681
     [Google Scholar]
337. ChenY. GuarnieriM.T. VasilA.I. VasilM.L. MantC.T. HodgesR.S. Role of peptide hydrophobicity in the mechanism of action of α-helical antimicrobial peptides.Antimicrob. Agents Chemother.20075141398140610.1128/AAC.00925‑06 17158938
     [Google Scholar]
338. GranL. An oxytocic principle found in oldenlandia affinis DC.Medd. Nor. Farm. Selsk.19701280
     [Google Scholar]
339. GustafsonK.R. SowderR.C.II HendersonL.E. ParsonsI.C. KashmanY. CardellinaJ.H.II McMahonJ.B. BuckheitR.W.Jr PannellL.K. BoydM.R. Circulins A and B. Novel human immunodeficiency virus (HIV)-inhibitory macrocyclic peptides from the tropical tree Chassalia parvifolia.J. Am. Chem. Soc.1994116209337933810.1021/ja00099a064
     [Google Scholar]
340. IseliB. BollerT. NeuhausJ.M. The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity.Plant Physiol.1993103122122610.1104/pp.103.1.221 8208848
     [Google Scholar]
341. GrainL. Isolation of oxytocic peptides from Oldenlandia affinis by solvent extraction of tetraphenylborate complexes and chromatography on sephadex LH-20.Lloydia1973362207208 4744557
     [Google Scholar]
342. GouldA. CamareroJ.A. Cyclotides: Overview and biotechnological applications.ChemBioChem201718141350136310.1002/cbic.201700153 28544675
     [Google Scholar]
343. GranL. On the effect of a polypeptide isolated from “Kalata-Kalata” (Oldenlandia affinis DC) on the oestrogen dominated uterus.Acta Pharmacol. Toxicol.1973335-640040810.1111/j.1600‑0773.1973.tb01541.x 4801084
     [Google Scholar]
344. PothA.G. MylneJ.S. GrasslJ. LyonsR.E. MillarA.H. ColgraveM.L. CraikD.J. Cyclotides associate with leaf vasculature and are the products of a novel precursor in petunia (Solanaceae).J. Biol. Chem.201228732270332704610.1074/jbc.M112.370841 22700981
     [Google Scholar]
345. PräntingM. LöövC. BurmanR. GöranssonU. AnderssonD.I. The cyclotide cycloviolacin O2 from Viola odorata has potent bactericidal activity against Gram-negative bacteria.J. Antimicrob. Chemother.20106591964197110.1093/jac/dkq220 20558471
     [Google Scholar]
346. GildingE.K. JacksonM.A. PothA.G. HenriquesS.T. PrentisP.J. MahatmantoT. CraikD.J. Gene coevolution and regulation lock cyclic plant defence peptides to their targets.New Phytol.2016210271773010.1111/nph.13789 26668107
     [Google Scholar]
347. SlazakB. KapustaM. MalikS. BohdanowiczJ. KutaE. MalecP. GöranssonU. Immunolocalization of cyclotides in plant cells, tissues and organ supports their role in host defense.Planta201624451029104010.1007/s00425‑016‑2562‑y 27394154
     [Google Scholar]
348. SlazakB. KapustaM. StrömstedtA.A. SłomkaA. KrychowiakM. ShariatgorjiM. AndrénP.E. BohdanowiczJ. KutaE. GöranssonU. How does the sweet violet (Viola odorata L.) fight pathogens and pests - cyclotides as a comprehensive plant host defense system.Front. Plant Sci.20189129610.3389/fpls.2018.01296 30254654
     [Google Scholar]
349. SieniawskaE. LosR. BajT. MalmA. GlowniakK. Antimicrobial efficacy of Mutellina purpurea essential oil and α-pinene against Staphylococcus epidermidis grown in planktonic and biofilm cultures.Ind. Crops Prod.20135115215710.1016/j.indcrop.2013.09.001
     [Google Scholar]
350. ChicheL. ChicheJ.N. WhalenE. PresnellS. GersukV. DangK. AnguianoE. QuinnC. BurteyS. BerlandY. KaplanskiG. HarleJ.R. PascualV. ChaussabelD. Modular transcriptional repertoire analyses of adults with systemic lupus erythematosus reveal distinct type I and type II interferon signatures.Arthritis Rheumatol.20146661583159510.1002/art.38628 24644022
     [Google Scholar]
351. QuimioF.M.E. DalyN.L. CraikD.J. Circular proteins in plants: Solution structure of a novel macrocyclic trypsin inhibitor from Momordica cochinchinensis.J. Biol. Chem.200127625228752288210.1074/jbc.M101666200 11292835
     [Google Scholar]
352. HeitzA. HernandezJ.F. GagnonJ. HongT.T. PhamT.T.C. NguyenT.M. NguyenL.D. ChicheL. Solution structure of the squash trypsin inhibitor MCoTI-II. A new family for cyclic knottins.Biochemistry200140277973798310.1021/bi0106639 11434766
     [Google Scholar]
353. MellstrandS.T. SamuelssonG. Phoratoxin, a toxic protein from the mistletoe Phoradendron tomentosum subsp. macrophyllum (Loranthaceae). Improvements in the isolation procedure and further studies on the properties.Eur. J. Biochem.197332114314710.1111/j.1432‑1033.1973.tb02590.x 4687388
     [Google Scholar]
354. SaetherO. CraikD.J. CampbellI.D. SlettenK. JuulJ. NormanD.G. Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1.Biochemistry199534134147415810.1021/bi00013a002 7703226
     [Google Scholar]
355. CraigM.H. SnowR.W. SueurL.D. A climate-based distribution model of malaria transmission in sub-Saharan Africa.Parasitol. Today199915310511110.1016/S0169‑4758(99)01396‑4 10322323
     [Google Scholar]
356. VeerD.S.J. KanM.W. CraikD.J. Cyclotides: From structure to function.Chem. Rev.201911924123751242110.1021/acs.chemrev.9b00402 31829013
     [Google Scholar]
357. YeshakM.Y. BurmanR. AsresK. GöranssonU. Cyclotides from an extreme habitat: Characterization of cyclic peptides from Viola abyssinica of the Ethiopian highlands.J. Nat. Prod.201174472773110.1021/np100790f 21434649
     [Google Scholar]
358. GöranssonU. LuijendijkT. JohanssonS. BohlinL. ClaesonP. Seven novel macrocyclic polypeptides from Viola arvensis.J. Nat. Prod.199962228328610.1021/np9803878 10075760
     [Google Scholar]
359. CraikD.J. DalyN.L. BondT. WaineC. Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.J. Mol. Biol.199929451327133610.1006/jmbi.1999.3383 10600388
     [Google Scholar]
360. BurmanR. SvedlundE. FelthJ. HassanS. HerrmannA. ClarkR.J. CraikD.J. BohlinL. ClaesonP. GöranssonU. GullboJ. Evaluation of toxicity and antitumor activity of cycloviolacin O2 in mice.Biopolymers201094562663410.1002/bip.21408 20564012
     [Google Scholar]
361. BroussalisA.M. GöranssonU. CoussioJ.D. FerraroG. MartinoV. ClaesonP. First cyclotide from Hybanthus (Violaceae).Phytochemistry2001581475110.1016/S0031‑9422(01)00173‑X 11524112
     [Google Scholar]
362. RavipatiA.S. HenriquesS.T. PothA.G. KaasQ. WangC.K. ColgraveM.L. CraikD.J. Lysine-rich cyclotides: A new subclass of circular knotted proteins from violaceae.ACS Chem. Biol.201510112491250010.1021/acschembio.5b00454 26322745
     [Google Scholar]
363. BobeyA. PintoM. CilliE. LopesN. BolzaniV. A cyclotide isolated from noisettia orchidiflora (Violaceae).Planta Med.20188412/1394795210.1055/a‑0632‑2204 29843182
     [Google Scholar]
364. NiyomployP. ChanL.Y. HarveyP.J. PothA.G. ColgraveM.L. CraikD.J. Discovery and characterization of cyclotides from Rinorea species.J. Nat. Prod.201881112512252010.1021/acs.jnatprod.8b00572 30387611
     [Google Scholar]
365. KoehbachJ. AttahA.F. BergerA. HellingerR. KutchanT.M. CarpenterE.J. RolfM. SonibareM.A. MoodyJ.O. WongG.K.S. DesseinS. GregerH. GruberC.W. Cyclotide discovery in gentianales revisited—identification and characterization of cyclic cystine‐knot peptides and their phylogenetic distribution in Rubiaceae plants.Biopolymers2013100543845210.1002/bip.22328 23897543
     [Google Scholar]
366. FahradpourM. KeovP. TognolaC. SantamarinaP.E. McCormickP.J. GhassempourA. GruberC.W. Cyclotides isolated from an ipecac root extract antagonize the corticotropin releasing factor type 1 receptor.Front. Pharmacol.2017861610.3389/fphar.2017.00616 29033832
     [Google Scholar]
367. NguyenG.K.T. LimW.H. NguyenP.Q.T. TamJ.P. Novel cyclotides and uncyclotides with highly shortened precursors from Chassalia chartacea and effects of methionine oxidation on bioactivities.J. Biol. Chem.201228721175981760710.1074/jbc.M111.338970 22467870
     [Google Scholar]
368. CoxS.D. MannC.M. MarkhamJ.L. BellH.C. GustafsonJ.E. WarmingtonJ.R. WyllieS.G. The mode of antimicrobial action of the essential oil of Melaleuca alternifolia (tea tree oil).J. Appl. Microbiol.200088117017510.1046/j.1365‑2672.2000.00943.x 10735256
     [Google Scholar]
369. CunhaN.B. BarbosaA.E.A.D. AlmeidaD.R.G. PortoW.F. MaximianoM.R. ÁlvaresL.C.S. MunhozC.B.R. EugênioC.U.O. VianaA.A.B. FrancoO.L. DiasS.C. Cloning and characterization of novel cyclotides genes from South American plants.Biopolymers2016106678479510.1002/bip.22938 27554590
     [Google Scholar]
370. PintoM.F.S. SilvaO.N. VianaJ.C. PortoW.F. MiglioloL. B da CunhaN. GomesN.Jr FensterseiferI.C. ColgraveM.L. CraikD.J. DiasS.C. FrancoO.L. Characterization of a bioactive acyclotide from palicourea rigida.J. Nat. Prod.201679112767277310.1021/acs.jnatprod.6b00270 27809507
     [Google Scholar]
371. PintoM.F.S. FensterseiferI.C.M. MiglioloL. SousaD.A. CapdvilleD.G. ValenciaA.J.W. ColgraveM.L. CraikD.J. MagalhãesB.S. DiasS.C. FrancoO.L. Identification and structural characterization of novel cyclotide with activity against an insect pest of sugar cane.J. Biol. Chem.2012287113414710.1074/jbc.M111.294009 22074926
     [Google Scholar]
372. GerlachS.L. BurmanR. BohlinL. MondalD. GöranssonU. Isolation, characterization, and bioactivity of cyclotides from the Micronesian plant Psychotria leptothyrsa.J. Nat. Prod.20107371207121310.1021/np9007365 20575512
     [Google Scholar]
373. MahatmantoT. MylneJ.S. PothA.G. SwedbergJ.E. KaasQ. SchaeferH. CraikD.J. The evolution of momordica cyclic peptides.Mol. Biol. Evol.201532239240510.1093/molbev/msu307 25376175
     [Google Scholar]
374. DuQ. ChanL.Y. GildingE.K. HenriquesS.T. CondonN.D. RavipatiA.S. KaasQ. HuangY.H. CraikD.J. Discovery and mechanistic studies of cytotoxic cyclotides from the medicinal herb Hybanthus enneaspermus.J. Biol. Chem.202029532109111092510.1074/jbc.RA120.012627 32414842
     [Google Scholar]
375. BarbetaB.L. MarshallA.T. GillonA.D. CraikD.J. AndersonM.A. Plant cyclotides disrupt epithelial cells in the midgut of lepidopteran larvae.Proc. Natl. Acad. Sci.200810541221122510.1073/pnas.0710338104 18202177
     [Google Scholar]
376. DancewiczK. SlazakB. KiełkiewiczM. KapustaM. BohdanowiczJ. GabryśB. Behavioral and physiological effects of Viola spp. cyclotides on Myzus persicae (Sulz.).J. Insect Physiol.202012210402510.1016/j.jinsphys.2020.104025 32059835
     [Google Scholar]
377. SimonsenS.M. SandoL. RosengrenK.J. WangC.K. ColgraveM.L. DalyN.L. CraikD.J. Alanine scanning mutagenesis of the prototypic cyclotide reveals a cluster of residues essential for bioactivity.J. Biol. Chem.2008283159805981310.1074/jbc.M709303200 18258598
     [Google Scholar]
378. ColgraveM.L. KotzeA.C. IrelandD.C. WangC.K. CraikD.J. The anthelmintic activity of the cyclotides: Natural variants with enhanced activity.ChemBioChem20089121939194510.1002/cbic.200800174 18618891
     [Google Scholar]
379. WangC.K.L. ColgraveM.L. GustafsonK.R. IrelandD.C. GoranssonU. CraikD.J. Anti-HIV cyclotides from the Chinese medicinal herb Viola yedoensis.J. Nat. Prod.2008711475210.1021/np070393g 18081258
     [Google Scholar]
380. MulvennaJ.P. SandoL. CraikD.J. Processing of a 22 kDa precursor protein to produce the circular protein tricyclon A.Structure200513569170110.1016/j.str.2005.02.013 15893660
     [Google Scholar]
381. WangC.K.L. ClarkR.J. HarveyP.J. RosengrenJ.K. CemazarM. CraikD.J. The role of conserved Glu residue on cyclotide stability and activity: A structural and functional study of kalata B12, a naturally occurring Glu to Asp mutant.Biochemistry201150194077408610.1021/bi2004153 21466163
     [Google Scholar]
382. BurmanR. HerrmannA. TranR. KiveläJ.E. LomizeA. GullboJ. GöranssonU. Cytotoxic potency of small macrocyclic knot proteins: Structure-activity and mechanistic studies of native and chemically modified cyclotides.Org. Biomol. Chem.20119114306431410.1039/c0ob00966k 21491023
     [Google Scholar]
383. BurmanR. StrömstedtA.A. MalmstenM. GöranssonU. Cyclotide-membrane interactions: Defining factors of membrane binding, depletion and disruption.Biochim. Biophys. Acta Biomembr.20111808112665267310.1016/j.bbamem.2011.07.004 21787745
     [Google Scholar]
384. HerrmannA. BurmanR. MylneJ.S. KarlssonG. GullboJ. CraikD.J. ClarkR.J. GöranssonU. The alpine violet, Viola biflora, is a rich source of cyclotides with potent cytotoxicity.Phytochemistry200869493995210.1016/j.phytochem.2007.10.023 18191970
     [Google Scholar]
385. HeW. ChanL.Y. ZengG. DalyN.L. CraikD.J. TanN. Isolation and characterization of cytotoxic cyclotides from Viola philippica.Peptides20113281719172310.1016/j.peptides.2011.06.016 21723349
     [Google Scholar]
386. SandoL. HenriquesT.S. FoleyF. SimonsenS.M. DalyN.L. HallK.N. GustafsonK.R. AguilarM.I. CraikD.J. A synthetic mirror image of kalata B1 reveals that cyclotide activity is independent of a protein receptor.ChemBioChem201112162456246210.1002/cbic.201100450 21928440
     [Google Scholar]
387. IrelandD.C. WangC.K.L. WilsonJ.A. GustafsonK.R. CraikD.J. Cyclotides as natural anti‐HIV agents.Biopolymers2008901516010.1002/bip.20886 18008336
     [Google Scholar]
388. GranL. SlettenK. SkjeldalL. Cyclic peptides from Oldenlandia affinis DC. Molecular and biological properties.Chem. Biodivers.20085102014202210.1002/cbdv.200890184 18972522
     [Google Scholar]
389. GründemannC. KoehbachJ. HuberR. GruberC.W. Do plant cyclotides have potential as immunosuppressant peptides?J. Nat. Prod.201275216717410.1021/np200722w 22272797
     [Google Scholar]
390. NguyenP.Q.T. LuuT.T. BaiY. NguyenG.K.T. PervushinK. TamJ.P. Allotides: Proline-rich cystine knot α-amylase inhibitors from Allamanda cathartica.J. Nat. Prod.201578469570410.1021/np500866c 25832441
     [Google Scholar]
391. OjedaP.G. CardosoM.H. FrancoO.L. Pharmaceutical applications of cyclotides.Drug Discov. Today201924112152216110.1016/j.drudis.2019.09.010 31541712
     [Google Scholar]
392. CorrêaJ.A.F. EvangelistaA.G. NazarethT.M. LucianoF.B. Fundamentals on the molecular mechanism of action of antimicrobial peptides.Materialia2019810049410.1016/j.mtla.2019.100494
     [Google Scholar]
393. HuangY.H. ColgraveM.L. ClarkR.J. KotzeA.C. CraikD.J. Lysine-scanning mutagenesis reveals an amendable face of the cyclotide kalata B1 for the optimization of nematocidal activity.J. Biol. Chem.201028514107971080510.1074/jbc.M109.089854 20103593
     [Google Scholar]
394. HenriquesS.T. PeacockH. BenfieldA.H. WangC.K. CraikD.J. Is the mirror image a true reflection? intrinsic membrane chirality modulates peptide binding.J. Am. Chem. Soc.201914151204602046910.1021/jacs.9b11194 31765148
     [Google Scholar]
395. HenriquesS.T. HuangY.H. CastanhoM.A.R.B. BagatolliL.A. SonzaS. TachedjianG. DalyN.L. CraikD.J. Phosphatidylethanolamine binding is a conserved feature of cyclotide-membrane interactions.J. Biol. Chem.201228740336293364310.1074/jbc.M112.372011 22854971
     [Google Scholar]
396. SvangårdE. BurmanR. GunasekeraS. LövborgH. GullboJ. GöranssonU. Mechanism of action of cytotoxic cyclotides: Cycloviolacin O2 disrupts lipid membranes.J. Nat. Prod.200770464364710.1021/np070007v 17378610
     [Google Scholar]
397. HenriquesS.T. HuangY.H. ChaousisS. SaniM.A. PothA.G. SeparovicF. CraikD.J. The prototypic cyclotide kalata B1 has a unique mechanism of entering cells.Chem. Biol.20152281087109710.1016/j.chembiol.2015.07.012 26278183
     [Google Scholar]
398. KamimoriH. HallK. CraikD.J. AguilarM.I. Studies on the membrane interactions of the cyclotides kalata B1 and kalata B6 on model membrane systems by surface plasmon resonance.Anal. Biochem.2005337114915310.1016/j.ab.2004.10.028 15649388
     [Google Scholar]
399. ShenkarevZ.O. NadezhdinK.D. SobolV.A. SobolA.G. SkjeldalL. ArsenievA.S. Conformation and mode of membrane interaction in cyclotides.FEBS J.2006273122658267210.1111/j.1742‑4658.2006.05282.x 16817894
     [Google Scholar]
400. FurukawaT. SakaguchiN. ShimadaH. Two OsGASR genes, rice GAST homologue genes that are abundant in proliferating tissues, show different expression patterns in developing panicles.Genes Genet. Syst.200681317118010.1266/ggs.81.171 16905871
     [Google Scholar]
401. ZimmermannR. SakaiH. HochholdingerF. The gibberellic acid stimulated-like gene family in maize and its role in lateral root development.Plant Physiol.2009152135636510.1104/pp.109.149054 19926801
     [Google Scholar]
402. RibeiroO.S. FontaineV. MathieuV. ZhiriA. BaudouxD. StévignyC. SouardF. Antibacterial and cytotoxic activities of ten commercially available essential oils.Antibiotics202091071710.3390/antibiotics9100717 33092096
     [Google Scholar]
403. LimaO.M. IsepponB.A. NetoJ. DecuadroR.S. KidoE. CrovellaS. PandolfiV. Snakin: Structure, roles and applications of a plant antimicrobial peptide.Curr. Protein Pept. Sci.201718436837410.2174/1389203717666160619183140 27323806
     [Google Scholar]
404. BardanA. NizetV. GalloR.L. Antimicrobial peptides and the skin.Expert Opin. Biol. Ther.20044454354910.1517/14712598.4.4.543 15102603
     [Google Scholar]
405. AlmasiaN. BazziniA.A. HoppH.E. RovereV.C. Overexpression of snakin‐1 gene enhances resistance to Rhizoctonia solani and Erwinia carotovora in transgenic potato plants.Mol. Plant Pathol.20089332933810.1111/j.1364‑3703.2008.00469.x 18705874
     [Google Scholar]
406. AlmasiaN.I. MolinariM.P. MaronicheG.A. NahirñakV. BarónB.M.P. TabogaO.A. RovereV.C. Successful production of the potato antimicrobial peptide Snakin-1 in baculovirus-infected insect cells and development of specific antibodies.BMC Biotechnol.20171717510.1186/s12896‑017‑0401‑2 29121909
     [Google Scholar]
407. KovalskayaN. HammondR.W. Expression and functional characterization of the plant antimicrobial snakin-1 and defensin recombinant proteins.Protein Expr. Purif.2009631121710.1016/j.pep.2008.08.013 18824107
     [Google Scholar]
408. KuddusM.R. RumiF. TsutsumiM. TakahashiR. YamanoM. KamiyaM. KikukawaT. DemuraM. AizawaT. Expression, purification and characterization of the recombinant cysteine-rich antimicrobial peptide snakin-1 in Pichia pastoris.Protein Expr. Purif.2016122152210.1016/j.pep.2016.02.002 26854372
     [Google Scholar]
409. MohanS. Snakin genes from potato: Overexpression confers blackleg disease resistance: A thesis submitted in partial fulfilment of the requirements for the degree of doctor of philosophy (PhD) in plant biotechnology at Lincoln University, New Zealand,PhD Thesis, Lincoln University2011
     [Google Scholar]
410. HarrisP.W.R. YangS.H. MolinaA. LópezG. MiddleditchM. BrimbleM.A. Plant antimicrobial peptides snakin-1 and snakin-2: Chemical synthesis and insights into the disulfide connectivity.Chemistry201420175102511010.1002/chem.201303207 24644073
     [Google Scholar]
411. SolanillaL.E. ZornG.B. NovellaS. BolandV.J.A. PalenzuelaR.P. Susceptibility of listeria monocytogenes to antimicrobial peptides.FEMS Microbiol. Lett.2003226110110510.1016/S0378‑1097(03)00579‑2 13129614
     [Google Scholar]
412. SilversteinK.A.T. MoskalW.A.Jr WuH.C. UnderwoodB.A. GrahamM.A. TownC.D. VandenBoschK.A. Small cysteine‐rich peptides resembling antimicrobial peptides have been under‐predicted in plants.Plant J.200751226228010.1111/j.1365‑313X.2007.03136.x 17565583
     [Google Scholar]
413. SolanillaL.E. OlmedoG.F. PalenzuelaR.P. Inactivation of the sapA to sapF locus of Erwinia chrysanthemi reveals common features in plant and animal bacterial pathogenesis.Plant Cell199810691792410.1105/tpc.10.6.917 9634580
     [Google Scholar]
414. MeiyalaghanS. ThomsonS.J. FiersM.W.E.J. BarrellP.J. LatimerJ.M. MohanS. JonesE.E. ConnerA.J. JacobsJ.M.E. Structure and expression of GSL1 and GSL2 genes encoding gibberellin stimulated-like proteins in diploid and highly heterozygous tetraploid potato reveals their highly conserved and essential status.BMC Genomics2014151210.1186/1471‑2164‑15‑2 24382166
     [Google Scholar]
415. MohanS. MeiyalaghanS. LatimerJ.M. GatehouseM.L. MonaghanK.S. VangaB.R. PitmanA.R. JonesE.E. ConnerA.J. JacobsJ.M.E. GSL2 over-expression confers resistance to Pectobacterium atrosepticum in potato.Theor. Appl. Genet.2014127367768910.1007/s00122‑013‑2250‑2 24370960
     [Google Scholar]
416. KovalskayaN. ZhaoY. HammondR.W. Antibacterial and antifungal activity of a snakin-defensin hybrid protein expressed in tobacco and potato plants.Open Plant Sci. J.201151294210.2174/1874294701105010029
     [Google Scholar]
417. ArivalaganS. ThomasN.S. ChandrasekaranB. ManiV. SiddiqueA.I. KuppsamyT. NamasivayamN. Combined therapeutic efficacy of carvacrol and X-radiation against 1,2-dimethyl hydrazine-induced experimental rat colon carcinogenesis.Mol. Cell. Biochem.20154101-2375410.1007/s11010‑015‑2536‑6 26264073
     [Google Scholar]
418. BalajiV. SessaG. SmartC.D. Silencing of host basal defense response-related gene expression increases susceptibility of Nicotiana benthamiana to Clavibacter michiganensis subsp. michiganensis.Phytopathology.201110133495710.1094/PHYTO‑05‑10‑013221062112
     [Google Scholar]
419. ShwaikiL.N. ArendtE.K. LynchK.M. Study on the characterisation and application of synthetic peptide Snakin-1 derived from potato tubers - action against food spoilage yeast.Food Control202011810736210.1016/j.foodcont.2020.107362
     [Google Scholar]
420. RongW. QiL. WangJ. DuL. XuH. WangA. ZhangZ. Expression of a potato antimicrobial peptide SN1 increases resistance to take-all pathogen Gaeumannomyces graminis var. tritici in transgenic wheat.Funct. Integr. Genomics201313340340910.1007/s10142‑013‑0332‑5 23839728
     [Google Scholar]
421. HerbelV. SchäferH. WinkM. Recombinant production of snakin-2 (an Antimicrobial Peptide from Tomato) in E. coli and analysis of its bioactivity.Molecules2015208148891490110.3390/molecules200814889 26287145
     [Google Scholar]
422. SuT. HanM. CaoD. XuM. Molecular and biological properties of snakins: The foremost cysteine-rich plant host defense peptides.J. Fungi20206422010.3390/jof6040220 33053707
     [Google Scholar]
423. DaneshmandF. ZardiniZ.H. EbrahimiL. Investigation of the antimicrobial activities of Snakin-Z, a new cationic peptide derived from Zizyphus jujuba fruits.Nat. Prod. Res.201327242292229610.1080/14786419.2013.827192 23962183
     [Google Scholar]
424. SelitrennikoffC.P. Antifungal proteins.Appl. Environ. Microbiol.20016772883289410.1128/AEM.67.7.2883‑2894.2001 11425698
     [Google Scholar]
425. TranD. TranP.A. TangY-Q. YuanJ. ColeT. SelstedM.E. Homodimeric theta-defensins from rhesus macaque leukocytes: Isolation, synthesis, antimicrobial activities, and bacterial binding properties of the cyclic peptides.J. Biol. Chem.200227753079308410.1074/jbc.M109117200 11675394
     [Google Scholar]
426. AmadorV.C. SilvaS.C.A. VilelaL.M.B. LimaO.M. RêgoS.M. FilhoR.R.S. SilvaO.R.L. LemosA.B. OliveiraD.W.D. NetoF.J.R.C. CrovellaS. IsepponB.A.M. Lipid transfer proteins (LTPs)—structure, diversity and roles beyond antimicrobial activity.Antibiotics20211011128110.3390/antibiotics10111281 34827219
     [Google Scholar]
427. LarsenL.K. WintherJ.R. Surprisingly high stability of barley lipid transfer protein, LTP1, towards denaturant, heat and proteases.FEBS Lett.2001488314514810.1016/S0014‑5793(00)02424‑8 11163761
     [Google Scholar]
428. EdstamM.M. LaurilaM. HöglundA. RamanA. DahlströmK.M. SalminenT.A. EdqvistJ. BlomqvistK. Characterization of the GPI-anchored lipid transfer proteins in the moss Physcomitrella patens.Plant Physiol. Biochem.201475556910.1016/j.plaphy.2013.12.001 24374350
     [Google Scholar]
429. EdstamM.M. ViitanenL. SalminenT.A. EdqvistJ. Evolutionary history of the non-specific lipid transfer proteins.Mol. Plant20114694796410.1093/mp/ssr019 21486996
     [Google Scholar]
430. KaderJ.C. Proteins and the intracellular exchange of lipids.Biochim. Biophys. Acta Lipids Lipid Metab.19753801314410.1016/0005‑2760(75)90042‑9 804327
     [Google Scholar]
431. KaderJ.C. Lipid-transfer proteins in plants.Annu. Rev. Plant Physiol. Plant Mol. Biol.199647162765410.1146/annurev.arplant.47.1.627 15012303
     [Google Scholar]
432. EdqvistJ. BlomqvistK. NieuwlandJ. SalminenT.A. Plant lipid transfer proteins: Are we finally closing in on the roles of these enigmatic proteins?J. Lipid Res.20185981374138210.1194/jlr.R083139 29555656
     [Google Scholar]
433. BoutrotF. ChantretN. GautierM.F. Genome-wide analysis of the rice and arabidopsis non-specific lipid transfer protein (nsLtp) gene families and identification of wheat nsLtp genes by EST data mining.BMC Genomics2008918610.1186/1471‑2164‑9‑86 18291034
     [Google Scholar]
434. LiJ. GaoG. XuK. ChenB. YanG. LiF. QiaoJ. ZhangT. WuX. Genome-wide survey and expression analysis of the putative non-specific lipid transfer proteins in Brassica rapa L.PLoS One201491e8455610.1371/journal.pone.0084556 24497919
     [Google Scholar]
435. WeiK. ZhongX. Non-specific lipid transfer proteins in maize.BMC Plant Biol.201414128110.1186/s12870‑014‑0281‑8 25348423
     [Google Scholar]
436. KallaR. ShimamotoK. PotterR. NielsenP.S. LinnestadC. OlsenO.A. The promoter of the barley aleurone‐specific gene encoding a putative 7 kDa lipid transfer protein confers aleurone cell‐specific expression in transgenic rice.Plant J.19946684986010.1046/j.1365‑313X.1994.6060849.x 7849757
     [Google Scholar]
437. BoutrotF. GuiraoA. AlaryR. JoudrierP. GautierM.F. Wheat non-specific lipid transfer protein genes display a complex pattern of expression in developing seeds.Biochim. Biophys. Acta Gene Struct. Expr.20051730211412510.1016/j.bbaexp.2005.06.010 16061294
     [Google Scholar]
438. EstanyolJ.M. RüthG.F.X. PuigdomènechP. The eight-cysteine motif, a versatile structure in plant proteins.Plant Physiol. Biochem.200442535536510.1016/j.plaphy.2004.03.009 15191737
     [Google Scholar]
439. SelsJ. MathysJ. ConinckD.B.M.A. CammueB.P.A. BolleD.M.F.C. Plant pathogenesis-related (PR) proteins: A focus on PR peptides.Plant Physiol. Biochem.2008461194195010.1016/j.plaphy.2008.06.011 18674922
     [Google Scholar]
440. FinkinaE.I. MelnikovaD.N. BogdanovI.V. OvchinnikovaT.V. Lipid transfer proteins as components of the plant innate immune system: Structure, functions, and applications.Acta Nat.201682476110.32607/20758251‑2016‑8‑2‑47‑61 27437139
     [Google Scholar]
441. NawrotR. BarylskiJ. NowickiG. BroniarczykJ. BuchwaldW. JózefiakG.A. Plant antimicrobial peptides.Folia Microbiol.201459318119610.1007/s12223‑013‑0280‑4 24092498
     [Google Scholar]
442. SouzaA.A. CostaA.S. CamposD.C.O. BatistaA.H.M. SalesG.W.P. NogueiraN.A.P. AlvesK.M.M. SouzaC.A.N. OliveiraH.D. Lipid transfer protein isolated from noni seeds displays antibacterial activity in vitro and improves survival in lethal sepsis induced by CLP in mice.Biochimie201814991710.1016/j.biochi.2018.03.011 29577952
     [Google Scholar]
443. CruzL. RibeiroS. CarvalhoA. VasconcelosI. RodriguesR. CunhaM. GomesV. Isolation and partial characterization of a novel lipid transfer protein (LTP) and antifungal activity of peptides from chilli pepper seeds.Protein Pept. Lett.201017331131810.2174/092986610790780305 19508213
     [Google Scholar]
444. ZamanU. AbbasiA. Isolation, purification and characterization of a nonspecific lipid transfer protein from Cuminum cyminum.Phytochemistry200970897998710.1016/j.phytochem.2009.04.021 19473681
     [Google Scholar]
445. OoiL.S.M. TianL. SuM. HoW.S. SunS.S.M. ChungH.Y. WongH.N.C. OoiV.E.C. Isolation, characterization, molecular cloning and modeling of a new lipid transfer protein with antiviral and antiproliferative activities from Narcissus tazetta.Peptides200829122101210910.1016/j.peptides.2008.08.020 18824058
     [Google Scholar]
446. MelnikovaD.N. MineevK.S. FinkinaE.I. ArsenievA.S. OvchinnikovaT.V. A novel lipid transfer protein from the dill Anethum graveolens L.: Isolation, structure, heterologous expression, and functional characteristics.J. Pept. Sci.2016221596610.1002/psc.2840 26680443
     [Google Scholar]
447. KristensenA.K. BrunstedtJ. NielsenK.K. RoepstorffP. MikkelsenJ.D. Characterization of a new antifungal non-specific lipid transfer protein (nsLTP) from sugar beet leaves.Plant Sci.20001551314010.1016/S0168‑9452(00)00190‑4 10773337
     [Google Scholar]
448. SchmittA.J. SathoffA.E. HollC. BauerB. SamacD.A. CarterC.J. The major nectar protein of Brassica rapa is a non-specific lipid transfer protein, BrLTP2.1, with strong antifungal activity.J. Exp. Bot.201869225587559710.1093/jxb/ery319 30169819
     [Google Scholar]
449. NawrotR. JózefiakD. SipA. KuźmaD. MusidlakO. JózefiakG.A. Isolation and characterization of a non-specific lipid transfer protein from Chelidonium majus L. latex.Int. J. Biol. Macromol.2017104Pt A55456310.1016/j.ijbiomac.2017.06.05728619636
     [Google Scholar]
450. BardV.G.C. NascimentoV.V. RibeiroS.F.F. RodriguesR. PeralesJ. FerreiraT.A. CarvalhoA.O. FernandesK.V.S. GomesV.M. Characterization of peptides from capsicum annuum hybrid seeds with inhibitory activity against α-amylase, serine proteinases and fungi.Protein J.201534212212910.1007/s10930‑015‑9604‑3 25750185
     [Google Scholar]
451. RegenteM.C. GiudiciA.M. VillalaínJ. CanalL. The cytotoxic properties of a plant lipid transfer protein involve membrane permeabilization of target cells.Lett. Appl. Microbiol.200540318318910.1111/j.1472‑765X.2004.01647.x 15715642
     [Google Scholar]
452. CamposD.C.O. CostaA.S. LimaA.D.R. SilvaF.D.A. LoboM.D.P. MoreiraM.A.C.O. MoreiraR.A. LealL.K.A.M. MironD. VasconcelosI.M. OliveiraH.D. First isolation and antinociceptive activity of a lipid transfer protein from noni (Morinda citrifolia) seeds.Int. J. Biol. Macromol.201686717910.1016/j.ijbiomac.2016.01.029 26783638
     [Google Scholar]
453. BogdanovI.V. ShenkarevZ.O. FinkinaE.I. MelnikovaD.N. RumynskiyE.I. ArsenievA.S. OvchinnikovaT.V. A novel lipid transfer protein from the pea Pisum sativum: Isolation, recombinant expression, solution structure, antifungal activity, lipid binding, and allergenic properties.BMC Plant Biol.201616110710.1186/s12870‑016‑0792‑6 27137920
     [Google Scholar]
454. NazeerM. WaheedH. SaeedM. AliS.Y. ChoudharyM.I. HaqU.Z. AhmedA. Purification and characterization of a nonspecific lipid transfer protein 1 (nsLTP1) from ajwain (Trachyspermum ammi) seeds.Sci. Rep.201991414810.1038/s41598‑019‑40574‑x 30858403
     [Google Scholar]
455. CasteelsP. RomagnoloJ. CastleM. JossonC.K. BromageE.H. TempstP. Biodiversity of apidaecin-type peptide antibiotics. Prospects of manipulating the antibacterial spectrum and combating acquired resistance.J. Biol. Chem.199426942261072611510.1016/S0021‑9258(18)47165‑7 7929322
     [Google Scholar]
456. JossonC.K. CapaciT. CasteelsP. TempstP. Apidaecin multipeptide precursor structure: A putative mechanism for amplification of the insect antibacterial response.EMBO J.19931241569157810.1002/j.1460‑2075.1993.tb05801.x 8467807
     [Google Scholar]
457. BroekaertW.F. MariënW. TerrasF.R.G. BolleD.M.F.C. ProostP. DammeV.J. DillenL. ClaeysM. ReesS.B. VanderleydenJ. Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins.Biochemistry199231174308431410.1021/bi00132a023 1567877
     [Google Scholar]
458. LeeD.G. ShinS.Y. KimD.H. SeoM.Y. KangJ.H. LeeY. KimK.L. HahmK.S. Antifungal mechanism of a cysteine-rich antimicrobial peptide, Ib-AMP1, from Impatiens balsamina against Candida albicans.Biotechnol. Lett.199921121047105010.1023/A:1005636610512
     [Google Scholar]
459. SlezinaM.P. OdintsovaT.I. Plant antimicrobial peptides: Insights into structure-function relationships for practical applications.Curr. Issues Mol. Biol.20234543674370410.3390/cimb45040239 37185763
     [Google Scholar]
460. PatelS.U. OsbornR. ReesS. ThorntonJ.M. Structural studies of Impatiens balsamina antimicrobial protein (Ib-AMP1).Biochemistry199837498399010.1021/bi971747d 9454588
     [Google Scholar]
461. FanX. ReichlingJ. WinkM. Antibacterial activity of the recombinant antimicrobial peptide Ib-AMP4 from Impatiens balsamina and its synergy with other antimicrobial agents against drug resistant bacteria.Pharmazie2013687628630 23923648
     [Google Scholar]
462. FanX. SchäferH. ReichlingJ. WinkM. Bactericidal properties of the antimicrobial peptide Ib‐AMP4 from Impatiens balsamina produced as a recombinant fusion‐protein in Escherichia coli.Biotechnol. J.20138101213122010.1002/biot.201300121 23713064
     [Google Scholar]
463. WuW.H. DiR. MatthewsK.R. Antibacterial mode of action of Ib-AMP1 against escherichia coli O157:H7.Probiotics Antimicrob. Proteins20135213114110.1007/s12602‑013‑9127‑1 26782738
     [Google Scholar]
464. WalujonoK. ScholmaR.A. BeintemaJ.J. AntonM. HahnA.M. Amino acid sequence of Hevein [of latex].In: International Rubber ConferenceKuala Lumpur (Malaysia),1975
     [Google Scholar]
465. ChapotM.P. PeumansW.J. StrosbergA.D. Extensive homologies between lectins from non‐leguminous plants.FEBS Lett.19861951-223123410.1016/0014‑5793(86)80166‑1
     [Google Scholar]
466. SlavokhotovaA.A. NaumannT.A. PriceN.P.J. RogozhinE.A. AndreevY.A. VassilevskiA.A. OdintsovaT.I. Novel mode of action of plant defense peptides - hevein‐like antimicrobial peptides from wheat inhibit fungal metalloproteases.FEBS J.2014281204754476410.1111/febs.13015 25154438
     [Google Scholar]
467. AndersenN.H. CaoB. RomeroR.A. ArreguinB. Hevein: NMR assignment and assessment of solution-state folding for the agglutinin-toxin motif.Biochemistry19933261407142210.1021/bi00057a004 8431421
     [Google Scholar]
468. ArcherB.L. The proteins of Hevea brasiliensis latex. 4. Isolation and characterization of crystalline hevein.Biochem. J.196075223624010.1042/bj0750236 13794068
     [Google Scholar]
469. GalelliA. BachiT.P. Urtica dioica agglutinin. A superantigenic lectin from stinging nettle rhizome.J. Immunol.1993151418211831
     [Google Scholar]
470. BarberoJ.J. CañadaJ.F. AsensioJ.L. AboitizN. VidalP. CanalesA. GrovesP. GabiusH.J. SiebertH.C. Hevein domains: An attractive model to study carbohydrate-protein interactions at atomic resolution.Adv. Carbohydr. Chem. Biochem.20066030335410.1016/S0065‑2318(06)60007‑3 16750446
     [Google Scholar]
471. PeralesD.A. ColladaC. BlancoC. MongeS.R. CarrilloT. AragoncilloC. SalcedoG. Cross-reactions in the latex-fruit syndrome: A relevant role of chitinases but not of complex asparagine-linked glycans.J. Allergy Clin. Immunol.1999104368168710.1016/S0091‑6749(99)70342‑8 10482846
     [Google Scholar]
472. KiniS.G. NguyenP.Q.T. WeissbachS. MallagarayA. ShinJ. YoonH.S. TamJ.P. Studies on the chitin binding property of novel cysteine-rich peptides from Alternanthera sessilis.Biochemistry201554436639664910.1021/acs.biochem.5b00872 26467613
     [Google Scholar]
473. EgorovT.A. OdintsovaT.I. Defense peptides of plant immunity.Russ. J. Bioorganic Chem.20123811910.1134/S1068162012010062
     [Google Scholar]
474. AndreevY.A. KorostylevaT.V. SlavokhotovaA.A. RogozhinE.A. UtkinaL.L. VassilevskiA.A. GrishinE.V. EgorovT.A. OdintsovaT.I. Genes encoding hevein-like defense peptides in wheat: Distribution, evolution, and role in stress response.Biochimie20129441009101610.1016/j.biochi.2011.12.023 22227377
     [Google Scholar]
475. BeintemaJ.J. Structural features of plant chitinases and chitin‐binding proteins.FEBS Lett.19943502-315916310.1016/0014‑5793(94)00753‑5 8070556
     [Google Scholar]
476. AsensioJ.L. SiebertH-C. von Der LiethC-W. LaynezJ. BruixM. SoedjanaamadjaU.M. BeintemaJ.J. CañadaF.J. GabiusH.J. BarberoJ.J. NMR investigations of protein-carbohydrate interactions: Studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N′,N”-triacetylchitotriose.Proteins200040221823610.1002/(SICI)1097‑0134(20000801)40:2<218::AID‑PROT50>3.0.CO;2‑P 10842338
     [Google Scholar]
477. NielsenS.B. OtzenD.E. Impact of the antimicrobial peptide Novicidin on membrane structure and integrity.J. Colloid Interface Sci.2010345224825610.1016/j.jcis.2010.01.065 20153477
     [Google Scholar]
478. HuangX. XieW. GongZ. Characteristics and antifungal activity of a chitin binding protein from Ginkgo biloba.FEBS Lett.20004781-212312610.1016/S0014‑5793(00)01834‑2 10922482
     [Google Scholar]
479. RogozhinE. RyazantsevD. SmirnovA. ZavrievS. Primary structure analysis of antifungal peptides from cultivated and wild cereals.Plants2018737410.3390/plants7030074 30213105
     [Google Scholar]
480. LiS.S. ClaesonP. Cys/Gly-rich proteins with a putative single chitin-binding domain from oat (Avena sativa) seeds.Phytochemistry200363324925510.1016/S0031‑9422(03)00116‑X 12737975
     [Google Scholar]
481. Van den BerghK. DammeE. PeumansW. CoosemansJ. Ee-CBP, a Hevein-Type antimicrobial peptide from bark of the spindle tree (Euonymus Europaeus L.).Mededel.200267327331
     [Google Scholar]
482. UtkinaL.L. AndreevY.A. RogozhinE.A. KorostylevaT.V. SlavokhotovaA.A. OparinP.B. VassilevskiA.A. GrishinE.V. EgorovT.A. OdintsovaT.I. Genes encoding 4‐Cys antimicrobial peptides in wheatT riticum kiharae Dorof. et Migush.: Multimodular structural organization, instraspecific variability, distribution and role in defence.FEBS J.2013280153594360810.1111/febs.12349 23702306
     [Google Scholar]
483. OdintsovaT.I. VassilevskiA.A. SlavokhotovaA.A. MusolyamovA.K. FinkinaE.I. KhadeevaN.V. RogozhinE.A. KorostylevaT.V. PukhalskyV.A. GrishinE.V. EgorovT.A. A novel antifungal hevein‐type peptide from Triticum kiharae seeds with a unique 10‐cysteine motif.FEBS J.2009276154266427510.1111/j.1742‑4658.2009.07135.x 19583772
     [Google Scholar]
484. ChávezM.I. PerellóV.M. CañadaF.J. AndreuD. BarberoJ.J. Effect of a serine-to-aspartate replacement on the recognition of chitin oligosaccharides by truncated hevein. A 3D view by using NMR.Carbohydr. Res.2010345101461146810.1016/j.carres.2010.02.019 20303073
     [Google Scholar]
485. EspinosaJ.F. AsensioJ.L. GarcíaJ.L. LaynezJ. BruixM. WrightC. SiebertH.C. GabiusH.J. CañadaF.J. BarberoJ.J. NMR investigations of protein-carbohydrate interactions.Eur. J. Biochem.2000267133965397810.1046/j.1432‑1327.2000.01415.x 10866795
     [Google Scholar]
486. IyerS. AcharyaK.R. Tying the knot: The cystine signature and molecular‐recognition processes of the vascular endothelial growth factor family of angiogenic cytokines.FEBS J.2011278224304432210.1111/j.1742‑4658.2011.08350.x 21917115
     [Google Scholar]
487. ReesD.C. LipscombW.N. Structure of the potato inhibitor complex of carboxypeptidase A at 2.5-A resolution.Proc. Natl. Acad. Sci.19807784633463710.1073/pnas.77.8.4633 6933511
     [Google Scholar]
488. HassG.M. HermodsonM.A. Amino acid sequence of a carboxypeptidase inhibitor from tomato fruit.Biochemistry19812082256226010.1021/bi00511a029 7236596
     [Google Scholar]
489. PearJ.R. RidgeN. RasmusgenR. RoseR.E. HouckC.M. Isolation and characterization of a fruit-specific cDNA and the corresponding genomic clone from tomato.Plant Mol. Biol.198913663965110.1007/BF00016019 2491680
     [Google Scholar]
490. MolnárA. LovasÁ. BánfalviZ. LakatosL. PolgárZ. HorváthS. Tissue-specific signal(s) activate the promoter of a metallocarboxypeptidase inhibitor gene family in potato tuber and berry.Plant Mol. Biol.200146330131110.1023/A:1010649503229 11488477
     [Google Scholar]
491. HeW.J. ChanL.Y. ClarkR.J. TangJ. ZengG.Z. FrancoO.L. CantacessiC. CraikD.J. DalyN.L. TanN.H. Novel inhibitor cystine knot peptides from Momordica charantia.PLoS One2013810e7533410.1371/journal.pone.0075334 24116036
     [Google Scholar]
492. ChanL.Y. HeW. TanN. ZengG. CraikD.J. DalyN.L. A new family of cystine knot peptides from the seeds of Momordica cochinchinensis.Peptides201339293510.1016/j.peptides.2012.09.018 23127518
     [Google Scholar]
493. NguyenP.Q.T. WangS. KumarA. YapL.J. LuuT.T. LescarJ. TamJ.P. Discovery and characterization of pseudocyclic cystine‐knot α‐amylase inhibitors with high resistance to heat and proteolytic degradation.FEBS J.2014281194351436610.1111/febs.12939 25040200
     [Google Scholar]
494. GracyJ. NguyenL.D. GellyJ-C. KaasQ. HeitzA. ChicheL. KNOTTIN: The knottin or inhibitor cystine knot scaffold in 2007.Nucleic Acids Res.200836Database issueD314D319 18025039
     [Google Scholar]
495. GellyJ.C. GracyJ. KaasQ. NguyenL.D. HeitzA. ChicheL. The KNOTTIN website and database: A new information system dedicated to the knottin scaffold.Nucleic Acids Res.20043290001156D15910.1093/nar/gkh015 14681383
     [Google Scholar]
496. QuilisJ. GarcíaL.B. MeynardD. GuiderdoniE. SegundoS.B. Inducible expression of a fusion gene encoding two proteinase inhibitors leads to insect and pathogen resistance in transgenic rice.Plant Biotechnol. J.201412336737710.1111/pbi.12143 24237606
     [Google Scholar]
497. CavalliniC. TretteneM. DeganM. DelvaP. MolesiniB. MinuzP. PandolfiniT. Anti‐angiogenic effects of two cystine‐knot miniproteins from tomato fruit.Br. J. Pharmacol.201116261261127310.1111/j.1476‑5381.2010.01154.x 21175567
     [Google Scholar]
498. TreggiariD. ZoccatelliG. MolesiniB. DeganM. RotinoG.L. SalaT. CavalliniC. MacRaeC.A. MinuzP. PandolfiniT. A cystine‐knot miniprotein from tomato fruit inhibits endothelial cell migration and angiogenesis by affecting vascular endothelial growth factor receptor (VEGFR) activation and nitric oxide production.Mol. Nutr. Food Res.201559112255226610.1002/mnfr.201500267 26255647
     [Google Scholar]
499. RodríguezG.J.J. ZarzosaO.A. GómezL.R. MezaL.J.E. Plant antimicrobial peptides as potential anticancer agents.BioMed Res. Int.2015201511110.1155/2015/735087 25815333
     [Google Scholar]
500. GruberC.W. ElliottA.G. IrelandD.C. DelpreteP.G. DesseinS. GöranssonU. TrabiM. WangC.K. KinghornA.B. RobbrechtE. CraikD.J. Distribution and evolution of circular miniproteins in flowering plants.Plant Cell20082092471248310.1105/tpc.108.062331 18827180
     [Google Scholar]
501. CraikD.J. Host-defense activities of cyclotides.Toxins20124213915610.3390/toxins4020139 22474571
     [Google Scholar]
502. JenningsC. WestJ. WaineC. CraikD. AndersonM. Biosynthesis and insecticidal properties of plant cyclotides: The cyclic knotted proteins from Oldenlandia affinis.Proc. Natl. Acad. Sci.20019819106141061910.1073/pnas.191366898 11535828
     [Google Scholar]
503. DuvickJ.P. RoodT. RaoA.G. MarshakD.R. Purification and characterization of a novel antimicrobial peptide from maize (Zea mays L.) kernels.J. Biol. Chem.199226726188141882010.1016/S0021‑9258(19)37034‑6 1527010
     [Google Scholar]
504. OparinP.B. MineevK.S. DunaevskyY.E. ArsenievA.S. BelozerskyM.A. GrishinE.V. EgorovT.A. VassilevskiA.A. Buckwheat trypsin inhibitor with helical hairpin structure belongs to a new family of plant defence peptides.Biochem. J.20124461697710.1042/BJ20120548 22612157
     [Google Scholar]
505. NoldeS.B. VassilevskiA.A. RogozhinE.A. BarinovN.A. BalashovaT.A. SamsonovaO.V. BaranovY.V. FeofanovA.V. EgorovT.A. ArsenievA.S. GrishinE.V. Disulfide-stabilized helical hairpin structure and activity of a novel antifungal peptide EcAMP1 from seeds of barnyard grass (Echinochloa crus-galli).J. Biol. Chem.201128628251452515310.1074/jbc.M110.200378 21561864
     [Google Scholar]
506. SlavokhotovaA.A. RogozhinE.A. Defense peptides from the α-hairpinin family are components of plant innate immunity.Front. Plant Sci.20201146510.3389/fpls.2020.00465 32391035
     [Google Scholar]
507. MarcusJ.P. GoulterK.C. MannersJ.M. Peptide fragments from plant vicilins expressed in escherichia coli exhibit antimicrobial activity in vitro.Plant Mol. Biol. Report.2008262758710.1007/s11105‑008‑0024‑9
     [Google Scholar]
508. ParkS.S. AbeK. KimuraM. UrisuA. YamasakiN. Primary structure and allergenic activity of trypsin inhibitors from the seeds of buckwheat (Fagopyrum esculentum Moench).FEBS Lett.1997400110310710.1016/S0014‑5793(96)01367‑1 9000522
     [Google Scholar]
509. CuiH. ZhangC. LiC. LinL. Inhibition mechanism of cardamom essential oil on methicillin-resistant Staphylococcus aureus biofilm.Lebensm. Wiss. Technol.202012210905710.1016/j.lwt.2020.109057
     [Google Scholar]
510. CuiZ. LiX. NishidaY. Synthesis and bioactivity of novel carvacrol and thymol derivatives containing 5-phenyl-2-furan.Lett. Drug Des. Discov.201411787788510.2174/1570180811666140220005252
     [Google Scholar]
511. ConnersR. KonarevA.V. ForsythJ. LovegroveA. MarshJ. HorneJ.T. ShewryP. BradyR.L. An unusual helix-turn-helix protease inhibitory motif in a novel trypsin inhibitor from seeds of Veronica (Veronica hederifolia L.).J. Biol. Chem.200728238277602776810.1074/jbc.M703871200 17640870
     [Google Scholar]
512. YamadaK. ShimadaT. KondoM. NishimuraM. NishimuraH.I. Multiple functional proteins are produced by cleaving Asn-Gln bonds of a single precursor by vacuolar processing enzyme.J. Biol. Chem.199927442563257010.1074/jbc.274.4.2563 9891029
     [Google Scholar]
513. KimuraM. ParkS.S. SakaiR. YamasakiN. FunatsuG. Primary structure of 6.5k-arginine/glutamate-rich polypeptide from the seeds of sponge gourd (Luffa cylindrica).Biosci. Biotechnol. Biochem.199761698498810.1271/bbb.61.984 9214759
     [Google Scholar]
514. FrenchG. Clinical impact and relevance of antibiotic resistance.Adv. Drug Deliv. Rev.200557101514152710.1016/j.addr.2005.04.005 15978698
     [Google Scholar]
515. BreithauptH. The new antibiotics.Nat. Biotechnol.199917121165116910.1038/70705 10585711
     [Google Scholar]
516. CassoneM. OtvosL.Jr Synergy among antibacterial peptides and between peptides and small-molecule antibiotics.Expert Rev. Anti Infect. Ther.20108670371610.1586/eri.10.38 20521897
     [Google Scholar]
517. BhattacharjyaS. RamamoorthyA. Multifunctional host defense peptides: Functional and mechanistic insights from NMR structures of potent antimicrobial peptides.FEBS J.2009276226465647310.1111/j.1742‑4658.2009.07357.x 19817858
     [Google Scholar]
518. HilchieA.L. WuerthK. HancockR.E.W. Immune modulation by multifaceted cationic host defense (antimicrobial) peptides.Nat. Chem. Biol.201391276176810.1038/nchembio.1393 24231617
     [Google Scholar]
519. AboyeT.L. StrömstedtA.A. GunasekeraS. BruhnJ.G. SeediE.H. RosengrenK.J. GöranssonU. A cactus-derived toxin-like cystine knot Peptide with selective antimicrobial activity.ChemBioChem20151671068107710.1002/cbic.201402704 25821084
     [Google Scholar]
520. GanzT. The role of antimicrobial peptides in innate immunity.Integr. Comp. Biol.200343230030410.1093/icb/43.2.300 21680437
     [Google Scholar]
521. ChoiK.Y. ChowL.N.Y. MookherjeeN. Cationic host defence peptides: Multifaceted role in immune modulation and inflammation.J. Innate Immun.20124436137010.1159/000336630 22739631
     [Google Scholar]
522. ShiW. HouT. GuoD. HeH. Evaluation of hypolipidemic peptide (Val-Phe-Val-Arg-Asn) virtual screened from chickpea peptides by pharmacophore model in high-fat diet-induced obese rat.J. Funct. Foods20195413614510.1016/j.jff.2019.01.001
     [Google Scholar]
523. PintoM.E.F. NajasJ.Z.G. MagalhãesL.G. BobeyA.F. MendonçaJ.N. LopesN.P. LemeF.M. TeixeiraS.P. TrovóM. AndricopuloA.D. KoehbachJ. GruberC.W. CilliE.M. BolzaniV.S. Inhibition of breast cancer cell migration by cyclotides isolated from Pombalia calceolaria.J. Nat. Prod.20188151203120810.1021/acs.jnatprod.7b00969 29757646
     [Google Scholar]
524. BhutiaS.K. PandaP.K. SinhaN. PraharajP.P. BholC.S. PanigrahiD.P. MahapatraK.K. SahaS. PatraS. MishraS.R. BeheraB.P. PatilS. MaitiT.K. Plant lectins in cancer therapeutics: Targeting apoptosis and autophagy-dependent cell death.Pharmacol. Res.201914481810.1016/j.phrs.2019.04.001 30951812
     [Google Scholar]
525. MukhopadhyayS. PandaP.K. DasD.N. SinhaN. BeheraB. MaitiT.K. BhutiaS.K. Abrus agglutinin suppresses human hepatocellular carcinoma in vitro and in vivo by inducing caspase-mediated cell death.Acta Pharmacol. Sin.201435681482410.1038/aps.2014.15 24793310
     [Google Scholar]