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Volume 2, Issue 1
  • ISSN: 2666-1217
  • E-ISSN: 2666-1225

Abstract

The development of antivenom or antidote requires the repetition of immunization of large animals, such as horses and goats, which ultimately releases the IgG immunoglobulin produced in the serum specimen. As snake venom involves a variety of proteins and enzymes getting administered into the animal, this process can inflict significant harm to the animal; therefore, choosing carriers that can deliver the least amount of venom could be a safer option for animal immunization.

In this research, nanoliposomes were used to encapsulate venom as a protected cargo for immunization. We used two distinct liposomal formulations to entrap the venom: 1,2-distearoyl-sn-glycero-3-phosphocholine, 1,2-distearoyl-sn-glycero-3-phospho-(1′-rac-glycerol) associated with cholesterol in one formulation and dimethyldioctadecylamonium (Bromide salt) paired with cholesterol in the other.

Liposomal formulations were prepared by a solvent evaporation method, and the venom was encapsulated in liposomes and evaluated for size and zeta potential. Meanwhile, encapsulation efficiency, venom release percentage, and phospholipase activity have all been analyzed.

The findings revealed that dimethyldioctadecylamonium (Bromide salt) combined with cholesterol had the highest encapsulation efficiency. In this formulation, the venom release rate had a steady-state profile. The lack of phospholipase activity in this formulation may be due to a bromide group in the liposomal structure that could be useful for immunization.

Liposomal formulations, which do not have the active site of the snake venom enzymes, could be used for venom encapsulation.

© 2022 Bentham Science Publishers
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/content/journals/vat/10.2174/2666121702666220106102156
2022-04-01
2025-03-02

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References

  1. GoswamiP.K. SamantM. SrivastavaR.S. Snake venom, anti-snake venom & potential of snake venom.Int. J. Pharm. Pharm. Sci.20146547
     [Google Scholar]
  2. IwanagaS. SuzukiT. Enzymes in snake venom.Springer197910.1007/978‑3‑642‑66913‑2_4
     [Google Scholar]
  3. LeeC. Snake venomsSpringer1979
     [Google Scholar]
  4. MoraisV. MassaldiH. Economic evaluation of snake antivenom production in the public system.J. Venom. Anim. Toxins Incl. Trop. Dis.200612349751110.1590/S1678‑91992006000300012
     [Google Scholar]
  5. MohammadpourD.N. DamavandiM. ZolfagharianH. MoradiS. Preparing and characterizing chitosan nanoparticles containing Hemiscorpius lepturus scorpion venom as an antigen delivery system.J. Venom. Anim. Toxins Incl. Trop. Dis.2012181445210.1590/S1678‑91992012000100006
     [Google Scholar]
  6. AkbarzadehA. Rezaei-SadabadyR. DavaranS. JooS.W. ZarghamiN. HanifehpourY. SamieiM. KouhiM. Nejati-KoshkiK. Liposome: Classification, preparation, and applications.Nanoscale Res. Lett.20138110210.1186/1556‑276X‑8‑10223432972
     [Google Scholar]
  7. SwensonS. CostaF. MineaR. SherwinR.P. ErnstW. FujiiG. YangD. MarklandF.S.Jr Intravenous liposomal delivery of the snake venom disintegrin contortrostatin limits breast cancer progression.Mol. Cancer Ther.20043449951115078994
     [Google Scholar]
  8. PanfoliI. RaveraS. CalziaD. DazziE. GandolfoS. PepeI.M. MorelliA. Inactivation of phospholipase A2 and metalloproteinase from Crotalus atrox venom by direct current.J. Biochem. Mol. Toxicol.200721171210.1002/jbt.2015217366544
     [Google Scholar]
  9. NkangaCI BapolisiAM OkaforNI KrauseRWM General perception of liposomes: Formation, manufacturing and applications.2019
     [Google Scholar]
  10. TorchilinP.V. TorchilinV. TorchilinV. WeissigV. Liposomes: A practical approach.Oxford, UKOxford University Press2003
     [Google Scholar]
  11. MarinettiG.V. The action of phospholipase A on lipoproteins.Biochim. Biophys. Acta196598355456510.1016/0005‑2760(65)90152‑95891200
     [Google Scholar]
  12. StábeliR.G. Simões-SilvaR. KayanoA.M. Purification of phospholipases A2 from American snake venoms. Chromatography—the Most Versatile Method of Chemical AnalysisIntech2012134
     [Google Scholar]
  13. KarrayA. FrikhaF. AliY.B. GargouriY. BezzineS. Purification and biochemical characterization of a secreted group IIA chicken intestinal phospholipase A 2.Lipids Health Dis.201110111210.1186/1476‑511X‑10‑27
     [Google Scholar]
  14. AhmedS.M. AhmedM. NadeemA. MahajanJ. ChoudharyA. PalJ. Emergency treatment of a snake bite: Pearls from literature.J. Emerg. Trauma Shock2008129710510.4103/0974‑2700.4319019561988
     [Google Scholar]
  15. ChienK-Y. ChiangC-M. HseuY-C. VyasA.A. RuleG.S. WuW. Two distinct types of cardiotoxin as revealed by the structure and activity relationship of their interaction with zwitterionic phospholipid dispersions.J. Biol. Chem.199426920144731448310.1016/S0021‑9258(17)36647‑48182052
     [Google Scholar]
  16. LallooD.G. TheakstonR.D. Snake antivenoms.J. Toxicol. Clin. Toxicol.2003413277290, 317-32710.1081/CLT‑12002111312807311
     [Google Scholar]
  17. LeónG. VargasM. SeguraÁ. HerreraM. VillaltaM. SánchezA. SolanoG. GómezA. SánchezM. EstradaR. GutiérrezJ.M. Current technology for the industrial manufacture of snake antivenoms.Toxicon2018151637310.1016/j.toxicon.2018.06.08429959968
     [Google Scholar]
  18. StormG. CrommelinD.J. Liposomes: quo vadis?Pharm. Sci. Technol. Today199811193110.1016/S1461‑5347(98)00007‑8
     [Google Scholar]
  19. WatsonD.S. EndsleyA.N. HuangL. Design considerations for liposomal vaccines: influence of formulation parameters on antibody and cell-mediated immune responses to liposome associated antigens.Vaccine201230132256227210.1016/j.vaccine.2012.01.07022306376
     [Google Scholar]
  20. FreitasT.V. FrézardF. Encapsulation of native crotoxin in liposomes: a safe approach for the production of antivenom and vaccination against Crotalus durissus terrificus venom.Toxicon19973519110010.1016/S0041‑0101(96)00061‑X9028012
     [Google Scholar]
  21. MorokumaK. KoboriN. FukudaT. UchidaT. SakaiA. ToribaM. OhkumaK. NakaiK. KurataT. TakahashiM. Experimental manufacture of equine antivenom against yamakagashi (Rhabdophis tigrinus).Jpn. J. Infect. Dis.201164539740221937821
     [Google Scholar]
  22. TheakstonR.D. ZumbuehlO. NewR.R. Use of liposomes for protective immunisation in sheep against Echis carinatus snake venom.Toxicon198523692192510.1016/0041‑0101(85)90384‑84095707
     [Google Scholar]
  23. BaxterL. YuanF. Interactions of liposomes with the biological milieu1994
     [Google Scholar]
  24. Bermúdez-MéndezE. Fuglsang-MadsenA. FønsS. LomonteB. GutiérrezJ.M. LaustsenA.H. Innovative immunization strategies for antivenom development.Toxins (Basel)2018101145210.3390/toxins1011045230400220
     [Google Scholar]
  25. ZhaoH. KinnunenP.K. Modulation of the activity of secretory phospholipase A2 by antimicrobial peptides.Antimicrob. Agents Chemother.200347396597110.1128/AAC.47.3.965‑971.200312604528
     [Google Scholar]
  26. LinderothL. AndresenT.L. JørgensenK. MadsenR. PetersG.H. Molecular basis of phospholipase A2 activity toward phospholipids with sn-1 substitutions.Biophys. J.2008941142610.1529/biophysj.107.11010617827229
     [Google Scholar]
  27. DavidsenJ. JørgensenK. AndresenT.L. MouritsenO.G. Secreted phospholipase A(2) as a new enzymatic trigger mechanism for localised liposomal drug release and absorption in diseased tissue.Biochim. Biophys. Acta2003160919510110.1016/S0005‑2736(02)00659‑412507763
     [Google Scholar]
  28. SongH. RamanadhamS. BaoS. HsuF-F. TurkJ. A bromoenol lactone suicide substrate inactivates group via phospholipase A2 by generating a diffusible bromomethyl keto acid that alkylates cysteine thiols.Biochemistry20064531061107310.1021/bi052065q16411783
     [Google Scholar]
  29. MeyerM.C. RastogiP. BeckettC.S. McHowatJ. Phospholipase A2 inhibitors as potential anti-inflammatory agents.Curr. Pharm. Des.200511101301131210.2174/138161205350752115853686
     [Google Scholar]
/content/journals/vat/10.2174/2666121702666220106102156
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Design, Fabrication and Characterization of Nanoliposomes Containing Snake Venom of Pseudocerastes persicus
Ven and Tox 2, e060122200043 (2022); https://doi.org/10.2174/2666121702666220106102156
/content/journals/vat/10.2174/2666121702666220106102156
/content/journals/vat/10.2174/2666121702666220106102156
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  • Article Type:     Research Article
Keyword(s): antivenom; immunization; nanoliposome; PLA2; Pseudocerastes persicus; Snake venom

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