Skip to content
2000
Volume 20, Issue 8
  • ISSN: 1573-4129
  • E-ISSN: 1875-676X

Abstract

Background and Objective

Lipopolysaccharide (LPS) is an essential constituent of the outer membrane of gram-negative bacteria, such as , and it plays a crucial role by inducing disease in the host. Penicillin-binding protein 1B (LpoB) is a key enzyme in the production of peptidoglycans, making it a potential target for the development of new antimicrobials. Flavonoids are naturally occurring plant-derived chemicals with a wide range of pharmacological properties, including antibacterial capabilities. The goal of this study was to identify the potential flavonoid that inhibits the protein LpoB using computational approaches and compare it with the standard antibiotic ciprofloxacin.

Methods

The study was carried out by selecting fifty flavonoids based on Lipinski’s rule of five. Molecular docking was carried out for selected flavonoids and ciprofloxacin against the LpoB protein using AutoDock 4. A 100 nanosecond molecular dynamic simulation was performed for apoprotein, LpoB-fisetin, and LpoB-ciprofloxacin complexes, followed by free energy calculation by Molecular Mechanics Generalized Born Surface Area (MMGBSA) solvation analysis.

Results

The docking results revealed that fisetin displayed five hydrogen bonds with a binding affinity of -4.67 kcal/mol, and ciprofloxacin exhibited a binding affinity of -4.36 kcal/mol with two hydrogen bonds. The apoprotein and fisetin complex remained stable throughout the 100 ns molecular dynamic simulation, while the ciprofloxacin complex lost its stability. The MMGBSA analysis with fisetin showed better binding free energy compared to ciprofloxacin.

Conclusion

The present study has emphasized the potential of flavonoids as probable candidates that can inhibit the protein LpoB. The integration of molecular docking, dynamic simulations, and MMGBSA analysis has provided significant insight into the thermodynamics and binding interactions of the LpoB- fisetin complex, and it has enabled further experimental validations.

© 2024 Bentham Science Publishers
Loading

Article metrics loading...

/content/journals/cpa/10.2174/0115734129335204240919071902
2024-09-24
2025-07-15

  • From This Site

    /content/journals/cpa/10.2174/0115734129335204240919071902
    dcterms_title,dcterms_subject,pub_keyword
    -contentType:Contributor -contentType:Concept -contentType:Institution
    10
    5
Loading full text...

Full text loading...

References

  1. MajowiczS.E. MustoJ. ScallanE. AnguloF.J. KirkM. O’BrienS.J. JonesT.F. FazilA. HoekstraR.M. International Collaboration on Enteric Disease ‘Burden of Illness’ Studies The global burden of nontyphoidal Salmonella gastroenteritis.Clin. Infect. Dis.201050688288910.1086/65073320158401
     [Google Scholar]
  2. SzilagyiA. GersonM. MendelsonJ. YusufN.A. Salmonella infections complicating inflammatory bowel disease.J. Clin. Gastroenterol.19857325125510.1097/00004836‑198506000‑000134020084
     [Google Scholar]
  3. EngS.K. PusparajahP. Ab MutalibN.S. SerH-L. ChanK-G. LeeL-H. Salmonella : A review on pathogenesis, epidemiology and antibiotic resistance.Front. Life Sci.20158328429310.1080/21553769.2015.1051243
     [Google Scholar]
  4. ChenH.M. WangY. SuL.H. ChiuC.H. Nontyphoid salmonella infection: Microbiology, clinical features, and antimicrobial therapy.Pediatr. Neonatol.201354314715210.1016/j.pedneo.2013.01.01023597525
     [Google Scholar]
  5. TsaiM.H. HuangY.C. LinT.Y. HuangY.L. KuoC.C. ChiuC.H. Reappraisal of parenteral antimicrobial therapy for nontyphoidal Salmonella enteric infection in children.Clin. Microbiol. Infect.201117230030510.1111/j.1469‑0691.2010.03230.x20384700
     [Google Scholar]
  6. ZhaL. GarrettS. SunJ. Salmonella infection in chronic inflammation and gastrointestinal cancer.Diseases2019712810.3390/diseases701002830857369
     [Google Scholar]
  7. MetchockB. In-vitro activity of azithromycin compared with other macrolides and oral antibiotics against Salmonella typhi. aJ. Antimicrob. Chemother.199025Suppl. A293110.1093/jac/25.suppl_A.292154435
     [Google Scholar]
  8. WHO (2010) Laboratory protocol ‘isolation of Salmonella spp. from food and animal faeces’. WHO Global Foodborne Infections Network (formerly WHO Global Salm-Surv) 5.
     [Google Scholar]
  9. Muthuirulandi SethuvelD.P. AnandanS. Devanga RagupathiN.K. VeeraraghavanB. VinodO. WaliaK. Association of blaCTX-M-15 and qnr genes in multidrug-resistant Salmonella Typhimurium and Shigella spp from India.J. Infect. Dev. Ctries.20159111294129710.3855/jidc.696526623641
     [Google Scholar]
  10. LipsitchM. SamoreM.H. Antimicrobial use and antimicrobial resistance: A population perspective.Emerg. Infect. Dis.20028434735410.3201/eid0804.01031211971765
     [Google Scholar]
  11. ChristakiE. MarcouM. TofaridesA. Antimicrobial resistance in bacteria: Mechanisms, evolution, and persistence.J. Mol. Evol.2020881264010.1007/s00239‑019‑09914‑331659373
     [Google Scholar]
  12. UddinT.M. ChakrabortyA.J. KhusroA. ZidanB.M.R.M. MitraS. EmranT.B. DhamaK. RiponM.K.H. GajdácsM. SahibzadaM.U.K. HossainM.J. KoiralaN. Antibiotic resistance in microbes: History, mechanisms, therapeutic strategies and future prospects.J. Infect. Public Health202114121750176610.1016/j.jiph.2021.10.02034756812
     [Google Scholar]
  13. YoneyamaH. KatsumataR. Antibiotic resistance in bacteria and its future for novel antibiotic development.Biosci. Biotechnol. Biochem.20067051060107510.1271/bbb.70.106016717405
     [Google Scholar]
  14. WiseR. A review of the mechanisms of action and resistance of antimicrobial agents.Can. Respir. J.19996Suppl. A20A22A10202228
     [Google Scholar]
  15. KapoorG. SaigalS. ElongavanA. Action and resistance mechanisms of antibiotics: A guide for clinicians.J. Anaesthesiol. Clin. Pharmacol.201733330030510.4103/joacp.JOACP_349_1529109626
     [Google Scholar]
  16. JacobJ.J. PragasamA.K. VasudevanK. VeeraraghavanB. KangG. JohnJ. NagvekarV. MutrejaA. Salmonella Typhi acquires diverse plasmids from other Enterobacteriaceae to develop cephalosporin resistance.Genomics202111342171217610.1016/j.ygeno.2021.05.00333965548
     [Google Scholar]
  17. JacobJ.J. SolaimalaiD. RachelT. PragasamA.K. SugumarS. JeslinP. AnandanS. VeeraraghavanB. A secular trend in invasive non-typhoidal Salmonella in South India, 2000–2020: Identification challenges and antibiogram.Indian J. Med. Microbiol.202240453654010.1016/j.ijmmb.2022.07.01535987666
     [Google Scholar]
  18. JacobJ.J. SolaimalaiD. Muthuirulandi SethuvelD.P. RachelT. JeslinP. AnandanS. VeeraraghavanB. A nineteen-year report of serotype and antimicrobial susceptibility of enteric non-typhoidal Salmonella from humans in Southern India: Changing facades of taxonomy and resistance trend.Gut Pathog.20201214910.1186/s13099‑020‑00388‑z33110449
     [Google Scholar]
  19. EdooZ. ArthurM. HugonnetJ.E. Reversible inactivation of a peptidoglycan transpeptidase by a β-lactam antibiotic mediated by β-lactam-ring recyclization in the enzyme active site.Sci. Rep.201771913610.1038/s41598‑017‑09341‑828831100
     [Google Scholar]
  20. AlenazyR. Antibiotic resistance in Salmonella: Targeting multidrug resistance by understanding efflux pumps, regulators and the inhibitors.J. King Saud Univ. Sci.202234710227510.1016/j.jksus.2022.102275
     [Google Scholar]
  21. KingD.T. LameignereE. StrynadkaN.C.J. Structural insights into the lipoprotein outer membrane regulator of penicillin-binding protein 1B.J. Biol. Chem.201428927192451925310.1074/jbc.M114.56587924808177
     [Google Scholar]
  22. EganA.J.F. JeanN.L. KoumoutsiA. BougaultC.M. BiboyJ. SassineJ. SolovyovaA.S. BreukinkE. TypasA. VollmerW. SimorreJ.P. Outer-membrane lipoprotein LpoB spans the periplasm to stimulate the peptidoglycan synthase PBP1B.Proc. Natl. Acad. Sci. USA2014111228197820210.1073/pnas.140037611124821816
     [Google Scholar]
  23. WiseE.M.Jr ParkJ.T. Penicillin: Its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis.Proc. Natl. Acad. Sci. USA1965541758110.1073/pnas.54.1.755216369
     [Google Scholar]
  24. GardeS. ChodisettiP.K. ReddyM. Peptidoglycan: Structure, synthesis, and regulation.Ecosal Plus202192ecosalplus.ESP-0010-202010.1128/ecosalplus.ESP‑0010‑202033470191
     [Google Scholar]
  25. GrayA.N. EganA.J.F. van’t VeerI.L. VerheulJ. ColavinA. KoumoutsiA. BiboyJ. AltelaarA.F.M. DamenM.J. HuangK.C. SimorreJ.P. BreukinkE. den BlaauwenT. TypasA. GrossC.A. VollmerW. Coordination of peptidoglycan synthesis and outer membrane constriction during Escherichia coli cell division.eLife20154e0711810.7554/eLife.0711825951518
     [Google Scholar]
  26. HattotuwagamaC.K. GuanP. DoytchinovaI.A. ZygouriC. FlowerD.R. Quantitative online prediction of peptide binding to the major histocompatibility complex.J. Mol. Graph. Model.200422319520710.1016/S1093‑3263(03)00160‑814629978
     [Google Scholar]
  27. JoshiT. JoshiT. SharmaP. ChandraS. PandeV. Molecular docking and molecular dynamics simulation approach to screen natural compounds for inhibition of Xanthomonas oryzae pv. Oryzae by targeting peptide deformylase.J. Biomol. Struct. Dyn.202139382384010.1080/07391102.2020.171920031965918
     [Google Scholar]
  28. TanZ. DengJ. YeQ. ZhangZ. The antibacterial activity of natural-derived flavonoids.Curr. Top. Med. Chem.202222121009101910.2174/156802662266622022111050635189804
     [Google Scholar]
  29. ElmaidomyA.H. ShadyN.H. AbdeljawadK.M. ElzamkanM.B. HelmyH.H. TarshanE.A. AdlyA.N. HussienY.H. SayedN.G. ZayedA. AbdelmohsenU.R. Antimicrobial potentials of natural products against multidrug resistance pathogens: A comprehensive review.RSC Advances20221245290782910210.1039/D2RA04884A36320761
     [Google Scholar]
  30. KongkhamB. PrabakaranD. PuttaswamyH. Opportunities and challenges in managing antibiotic resistance in bacteria using plant secondary metabolites.Fitoterapia202014710476210.1016/j.fitote.2020.10476233069839
     [Google Scholar]
  31. BuchmannD. SchwabeM. WeissR. KussA.W. SchauflerK. SchlüterR. RödigerS. GuentherS. SchultzeN. Natural phenolic compounds as biofilm inhibitors of multidrug-resistant Escherichia coli – the role of similar biological processes despite structural diversity.Front. Microbiol.202314123203910.3389/fmicb.2023.123203937731930
     [Google Scholar]
  32. VaouN. StavropoulouE. VoidarouC.C. TsakrisZ. RozosG. TsigalouC. BezirtzoglouE. Interactions between medical plant-derived bioactive compounds: Focus on antimicrobial combination effects.Antibiotics.2022118101410.3390/antibiotics1108101436009883
     [Google Scholar]
  33. HuangW. WangY. TianW. CuiX. TuP. LiJ. ShiS. LiuX. Biosynthesis investigations of terpenoid, alkaloid, and flavonoid antimicrobial agents derived from medicinal plants.Antibiotics.20221110138010.3390/antibiotics1110138036290037
     [Google Scholar]
  34. SharmaV. PanwarA. SharmaA.K. Molecular dynamic simulation study on chromones and flavonoids for the in silico designing of a potential ligand inhibiting mTOR pathway in breast cancer.Curr. Pharmacol. Rep.20206637337910.1007/s40495‑020‑00246‑1
     [Google Scholar]
  35. ZhongZ. ZhouS. LiangY. WeiY. LiY. LongT. HeQ. LiM. ZhouY. YuY. FangL. LiaoX. KreiswirthB.N. ChenL. RenH. LiuY. SunJ. Natural flavonoids disrupt bacterial iron homeostasis to potentiate colistin efficacy.Sci. Adv.2023923eadg420510.1126/sciadv.adg420537294761
     [Google Scholar]
  36. ShamsudinN.F. AhmedQ.U. MahmoodS. Ali ShahS.A. KhatibA. MukhtarS. AlsharifM.A. ParveenH. ZakariaZ.A. Antibacterial effects of flavonoids and their structure-activity relationship study: A comparative interpretation.Molecules2022274114910.3390/molecules2704114935208939
     [Google Scholar]
  37. HochmaE. YarmolinskyL. KhalfinB. NisnevitchM. Ben-ShabatS. NakonechnyF. Antimicrobial effect of phytochemicals from edible plants.Processes.2021911208910.3390/pr9112089
     [Google Scholar]
  38. JadimurthyR. JagadishS. NayakS.C. KumarS. MohanC.D. RangappaK.S. Phytochemicals as invaluable sources of potent antimicrobial agents to combat antibiotic resistance.Life.202313494810.3390/life1304094837109477
     [Google Scholar]
  39. AlSheikhH.M.A. SultanI. KumarV. RatherI.A. Al-SheikhH. Tasleem JanA. HaqQ.M.R. Plant‐based phytochemicals as possible alternative to antibiotics in combating bacterial drug resistance.Antibiotics.20209848010.3390/antibiotics908048032759771
     [Google Scholar]
  40. ThebtiA. MeddebA. Ben SalemI. BakaryC. AyariS. RezguiF. Essafi-BenkhadirK. BoudabousA. OuzariH.I. Antimicrobial activities and mode of flavonoid actions.Antibiotics.202312222510.3390/antibiotics1202022536830135
     [Google Scholar]
  41. DeepasreeK. SubhashreeV. Molecular docking and dynamic simulation studies of terpenoid compounds against phosphatidylinositol-specific phospholipase C from Listeria monocytogenes.Inform. Med. Unlocked20233910125210.1016/j.imu.2023.101252
     [Google Scholar]
  42. ValathoorM.N. VenugopalS. In silico analysis of structure and function of hypothetical proteins in Salmonella typhimurium (SL1344).Res. J. Pharm. Technol.2024170010010.52711/0974‑360X.2024.00100
     [Google Scholar]
  43. SubramaniN.K. VenugopalS. Molecular Docking and Dynamic Simulation Studies of Bioactive Compounds from Traditional Medicinal Compounds Against Exfoliative Toxin B from Staphylococcus aureus.J. Pharmacol. Pharmacother.2024126607210.1177/0976500X241266072
     [Google Scholar]
  44. BermanH.M. BattistuzT. BhatT.N. The protein data bank.Acta Crystallogr. D Biol. Crystallogr.20025810.1107/s0907444902003451
     [Google Scholar]
  45. MorrisG.M. RuthH. LindstromW. Software news and updates AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility.J. Comput. Chem.20093010.1002/jcc.21256
     [Google Scholar]
  46. TianW. ChenC. LeiX. ZhaoJ. LiangJ. CASTp 3.0: Computed atlas of surface topography of proteins.Nucleic Acids Res.201846W1W363W36710.1093/nar/gky47329860391
     [Google Scholar]
  47. KimS. Exploring chemical information in PubChem.Curr. Protoc.202118e21710.1002/cpz1.21734370395
     [Google Scholar]
  48. DainaA. MichielinO. ZoeteV. SwissADME: A free web tool to evaluate pharmacokinetics, drug-likeness and medicinal chemistry friendliness of small molecules.Sci. Rep.2017714271710.1038/srep4271728256516
     [Google Scholar]
  49. O’BoyleN.M. BanckM. JamesC.A. MorleyC. VandermeerschT. HutchisonG.R. Open Babel: An open chemical toolbox.J. Cheminform.2011313310.1186/1758‑2946‑3‑3321982300
     [Google Scholar]
  50. GopikrishnanM. George Priya DossC. Molecular docking and dynamic approach to screen the drug candidate against the Imipenem-resistant CarO porin in Acinetobacter baumannii.Microb. Pathog.202317710604910.1016/j.micpath.2023.10604936858184
     [Google Scholar]
  51. Biovia (2020) Biovia Discovery Studio® 2020: Comprehensive modeling and simulations for life sciences datasheet.Biovia Dassault Systemes: The 3D Experience Company.2020
     [Google Scholar]
  52. Van Der SpoelD. LindahlE. HessB. GroenhofG. MarkA.E. BerendsenH.J.C. GROMACS: Fast, flexible, and free.J. Comput. Chem.200526161701171810.1002/jcc.2029116211538
     [Google Scholar]
  53. Hephzibah CathrynR. George Priya DossC. Comparative molecular dynamics simulation of apo and holo forms of the P53 mutant C176F: A structural perspective.J. Taibah Univ. Sci.2024181229745710.1080/16583655.2023.2297457
     [Google Scholar]
  54. VanommeslaegheK. HatcherE. AcharyaC. KunduS. ZhongS. ShimJ. DarianE. GuvenchO. LopesP. VorobyovI. MackerellA.D.Jr CHARMM general force field: A force field for drug‐like molecules compatible with the CHARMM all‐atom additive biological force fields.J. Comput. Chem.201031467169010.1002/jcc.2136719575467
     [Google Scholar]
  55. ZoeteV. CuendetM.A. GrosdidierA. MichielinO. SwissParam: A fast force field generation tool for small organic molecules.J. Comput. Chem.201132112359236810.1002/jcc.2181621541964
     [Google Scholar]
  56. BerendsenH.J.C. PostmaJ.P.M. van GunsterenW.F. DiNolaA. HaakJ.R. Molecular dynamics with coupling to an external bath.J. Chem. Phys.19848183684369010.1063/1.448118
     [Google Scholar]
  57. AndersenH.C. Molecular dynamics simulations at constant pressure and/or temperature.J. Chem. Phys.19807242384239310.1063/1.439486
     [Google Scholar]
  58. KumariR. DalalV. Identification of potential inhibitors for LLM of Staphylococcus aureus : Structure-based pharmacophore modeling, molecular dynamics, and binding free energy studies.J. Biomol. Struct. Dyn.202240209833984710.1080/07391102.2021.193617934096457
     [Google Scholar]
  59. TP. KattaB. Lulu SS. SundararajanV. Gene expression analysis reveals GRIN1, SYT1, and SYN2 as significant therapeutic targets and drug repurposing reveals lorazepam and lorediplon as potent inhibitors to manage Alzheimer’s disease.J. Biomol. Struct. Dyn.202312210.1080/07391102.2023.225687837691428
     [Google Scholar]
  60. KushwahaP.P. SinghA.K. BansalT. YadavA. PrajapatiK.S. ShuaibM. KumarS. Identification of natural inhibitors against SARS-CoV-2 drugable targets using molecular docking, molecular dynamics simulation, and MM-PBSA approach.Front. Cell. Infect. Microbiol.20211173028810.3389/fcimb.2021.73028834458164
     [Google Scholar]
  61. Valdés-TresancoM.S. Valdés-TresancoM.E. ValienteP.A. MorenoE. gmx_MMPBSA: A New Tool to Perform End-State Free Energy Calculations with GROMACS.J. Chem. Theory Comput.202117106281629110.1021/acs.jctc.1c0064534586825
     [Google Scholar]
  62. KumariR. KumarR. LynnA. Open Source Drug Discovery Consortium g_mmpbsa--a GROMACS tool for high-throughput MM-PBSA calculations.J. Chem. Inf. Model.20145471951196210.1021/ci500020m24850022
     [Google Scholar]
  63. KumariR. KumarV. DhankharP. DalalV. Promising antivirals for PLpro of SARS-CoV-2 using virtual screening, molecular docking, dynamics, and MMPBSA.J. Biomol. Struct. Dyn.202341104650466610.1080/07391102.2022.207134035510600
     [Google Scholar]
  64. RathiR. KumariR. PathakS.R. DalalV. Promising antibacterials for LLM of Staphylococcus aureus using virtual screening, molecular docking, dynamics, and MMPBSA.J. Biomol. Struct. Dyn.202341157277728910.1080/07391102.2022.211927836073371
     [Google Scholar]
  65. KumariR. RathiR. PathakS.R. DalalV. Structural-based virtual screening and identification of novel potent antimicrobial compounds against YsxC of Staphylococcus aureus.J. Mol. Struct.2022125513247610.1016/j.molstruc.2022.132476
     [Google Scholar]
  66. BelloM. Evaluation of structural and thermodynamic insight of ERβ with DPN and derivatives through MMGBSA/MMPBSA methods.Steroids202420110933410.1016/j.steroids.2023.10933437949336
     [Google Scholar]
  67. LipinskiC.A. Lead- and drug-like compounds: The rule-of-five revolution.Drug Discov. Today. Technol.20041433734110.1016/j.ddtec.2004.11.00724981612
     [Google Scholar]
  68. BenetL.Z. HoseyC.M. UrsuO. BDDCS, the rule of 5 and drugability graphical abstract HHS public access.Adv. Drug Deliv. Rev.201610110.1016/j.addr.2016.05.007
     [Google Scholar]
  69. GłowackiE.D. Irimia-VladuM. BauerS. SariciftciN.S. Hydrogen-bonds in molecular solids – from biological systems to organic electronics.J. Mater. Chem. B Mater. Biol. Med.20131313742375310.1039/c3tb20193g32261127
     [Google Scholar]
  70. PatilR. DasS. StanleyA. YadavL. SudhakarA. VarmaA.K. Optimized hydrophobic interactions and hydrogen bonding at the target-ligand interface leads the pathways of drug-designing.PLoS One201058e1202910.1371/journal.pone.001202920808434
     [Google Scholar]
  71. KunduK. PushparaniD. Using In-Silico Molecular Docking as a Tool to Justify the Anti-Typhoid Property of Terminalia Chebula.Cohesive Journal of Microbiology and Infection Disease202300064110.31031/CJMI.2023.06.000641
     [Google Scholar]
  72. ChughA SehgalI KhuranaN Comparative docking studies of drugs and phytocompounds for emerging variants of SARS-CoV-23 Biotech20231310.1007/s13205‑022‑03450‑6
     [Google Scholar]
  73. AmejiP.J. UzairuA. ShallangwaG.A. UbaS. Molecular docking-based virtual screening, drug-likeness, and pharmacokinetic profiling of some anti-Salmonella typhimurium cephalosporin derivatives.J. Taibah Univ. Med. Sci.20231861417143110.1016/j.jtumed.2023.05.02138162870
     [Google Scholar]
  74. ElebijuO.F. OduseluG.O. OgunnupebiT.A. AjaniO.O. AdebiyiE. In Silico Design of Potential Small-Molecule Antibiotic Adjuvants against Salmonella typhimurium Ortho Acetyl Sulphydrylase Synthase to Address Antimicrobial Resistance.Pharmaceuticals.202417554310.3390/ph1705054338794114
     [Google Scholar]
  75. SamykannuG. VijayababuP. AntonyrajC.B. NarayananS.B. Basheer AhamedS.I. Investigations of binding mode insight in Salmonella typhi type-III secretion system tip protein (SipD): A molecular docking and MD simulation study.Inform. Med. Unlocked2017916617210.1016/j.imu.2017.08.002
     [Google Scholar]
  76. SalariaD. RoltaR. MehtaJ. AwofisayoO. FadareO.A. KaurB. KumarB. Araujo da CostaR. ChandelS.R. KaushikN. ChoiE.H. KaushikN.K. Phytoconstituents of traditional Himalayan Herbs as potential inhibitors of Human Papillomavirus (HPV-18) for cervical cancer treatment: An In silico Approach.PLoS One2022173e026542010.1371/journal.pone.026542035298541
     [Google Scholar]
  77. KumariR. RathiR. PathakS.R. DalalV. Computational investigation of potent inhibitors against YsxC: Structure-based pharmacophore modeling, molecular docking, molecular dynamics, and binding free energy.J. Biomol. Struct. Dyn.202341393094110.1080/07391102.2021.201544634913841
     [Google Scholar]
/content/journals/cpa/10.2174/0115734129335204240919071902
Loading
Molecular Docking and Dynamic Simulation Approach to Target Penicillin- Binding Protein 1B (LpoB) of Salmonella typhimurium with Flavonoids
Current Pharmaceutical Analysis 20, 849 (2024); https://doi.org/10.2174/0115734129335204240919071902
/content/journals/cpa/10.2174/0115734129335204240919071902
/content/journals/cpa/10.2174/0115734129335204240919071902
Loading

Data & Media loading...


  • Article Type:     Research Article
Keyword(s): dynamic simulation; Flavonoids; LpoB; MMGBSA; molecular docking; Salmonella typhimurium

Most Cited Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error
Please enter a valid_number test