Temperature effect in the inhibition of PLA₂ activity of Bothrops brazili venom by Rosmarinic and Chlorogenic acids, experimental and computational approaches

References

• Abraham, M. J., Murtola, T., Schulz, R., Páll, S., Smith, J. C., Hess, B., & Lindah, E. (2015). Gromacs: High performance molecular simulations through multi-level parallelism from laptops to supercomputers. SoftwareX, 1-2, 19–25. https://doi.org/10.1016/j.softx.2015.06.001
   Google Scholar
• Adrião, A. A. X., dos Santos, A. O., de Lima, E. J. S. P., Maciel, J. B., Paz, W. H. P., da Silva, F. M. A., Pucca, M. B., Moura-da-Silva, A. M., Monteiro, W. M., Sartim, M. A., & Koolen, H. H. F. (2022). Plant-derived toxin inhibitors as potential candidates to complement antivenom treatment in snakebite envenomations. Frontiers in Immunology, 13(May), 842576. https://doi.org/10.3389/fimmu.2022.842576
   PubMedGoogle Scholar
• Aiswarya, N., Remya, C., Remashree, A. B., Sadasivan, C., & Dileep, K. V. (2022). Binding of rosmarinic acid curcumin and capsaicin with PLA2: A comparative study. Biochemical and Biophysical Research Communications, 626, 187–191. https://doi.org/10.1016/j.bbrc.2022.08.028
   PubMed Web of Science ®Google Scholar
• Arni, R. K., & Ward, R. J. (1996). Phospholipase A2—A structural review. Toxicon: Official Journal of the International Society on Toxinology, 34(8), 827–841. https://doi.org/10.1016/0041-0101(96)00036-0
   PubMed Web of Science ®Google Scholar
• Berendsen, H. J. C., Postma, J. P. M., Van Gunsteren, W. F., Dinola, A., & Haak, J. R. (1984). Molecular dynamics with coupling to an external bath. The Journal of Chemical Physics, 81(8), 3684–3690. https://doi.org/10.1063/1.448118
   Web of Science ®Google Scholar
• Bertoni, M., Kiefer, F., Biasini, M., Bordoli, L., & Schwede, T. (2017). Modeling protein quaternary structure of homo- and hetero-oligomers beyond binary interactions by homology. Scientific Reports, 7(1), 1–15. https://doi.org/10.1038/s41598-017-09654-8
   PubMedGoogle Scholar
• Borges, R. J., Lemke, N., & Fontes, M. R. M. (2017). PLA2-like proteins myotoxic mechanism: A dynamic model description. Scientific Reports, 7(1), 1–12. https://doi.org/10.1038/s41598-017-15614-z
   PubMedGoogle Scholar
• Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72(1-2), 248–254. https://doi.org/10.1016/0003-2697(76)90527-3
   PubMed Web of Science ®Google Scholar
• Bussi, G., Donadio, D., & Parrinello, M. (2007). Canonical sampling through velocity rescaling. The Journal of Chemical Physics, 126(1), 014101. https://doi.org/10.1063/1.2408420
   PubMed Web of Science ®Google Scholar
• Cardoso, F. F., Gomes, A. A. S., Dreyer, T. R., Cavalcante, W. L. G., Dal Pai, M., Gallacci, M., & Fontes, M. R. M. (2020). Neutralization of a bothropic PLA2-like protein by caftaric acid, a novel potent inhibitor of ophidian myotoxicity. Biochimie, 170, 163–172. https://doi.org/10.1016/j.biochi.2020.01.010
   PubMed Web of Science ®Google Scholar
• Chandrasekaran, R., Bhattacharjee, A., & Devadasan, V. (2019). Anti-inflammatory and Antidote Drug Discovery with Secreted Phospholipase A2 BT - Biocatalysis: Enzymatic Basics and Applications (Q. Husain & M. F. Ullah (eds.), pp. 193–211). Springer International Publishing. https://doi.org/10.1007/978-3-030-25023-2_10
   Google Scholar
• Chaves, L. F., Chuang, T. W., Sasa, M., & Gutiérrez, J. M. (2015). Snakebites are associated with poverty, weather fluctuations, and El Niño. Science Advances, 1(8), e1500249. https://doi.org/10.1126/sciadv.1500249
   Web of Science ®Google Scholar
• Chinnasamy, S., Selvaraj, G., Selvaraj, C., Kaushik, A. C., Kaliamurthi, S., Khan, A., Singh, S. K., & Wei, D. Q. (2020). Combining in silico and in vitro approaches to identification of potent inhibitor against phospholipase A2 (PLA2). International Journal of Biological Macromolecules, 144, 53–66. https://doi.org/10.1016/j.ijbiomac.2019.12.091
   PubMed Web of Science ®Google Scholar
• Chippaux, J. P. (2011). Estimate of the burden of snakebites in sub-Saharan Africa: A meta-analytic approach. Toxicon, 57(4), 586–599. https://doi.org/10.1016/j.toxicon.2010.12.022
   PubMed Web of Science ®Google Scholar
• Chippaux, J. P. (2017). Snakebite envenomation turns again into a neglected tropical disease! Journal of Venomous Animals and Toxins Including Tropical Diseases, 23(1), 38-40. https://doi.org/10.1186/s40409-017-0127-6
   Google Scholar
• Cristino, J. S., Salazar, G. M., Machado, V. A., Honorato, E., Farias, A. S., Vissoci, J. R. N., Neto, A. V. S., Lacerda, M., Wen, F. H., Monteiro, W. M., & Sachett, J. A. G. (2021). A painful journey to antivenom: The therapeutic itinerary of snakebite patients in the Brazilian Amazon (The QUALISnake Study). PLoS Neglected Tropical Diseases, 15(3), e0009245. https://doi.org/10.1371/journal.pntd.0009245
   PubMed Web of Science ®Google Scholar
• Dennis, E. A., Cao, J., Hsu, Y. H., Magrioti, V., & Kokotos, G. (2011). Phospholipase A2 enzymes: Physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention. Chemical Reviews, 111(10), 6130–6185. https://doi.org/10.1021/cr200085w
   PubMed Web of Science ®Google Scholar
• Devi, A., Namsa, N. D., & Doley, R. (2020). In silico and in vitro neutralization of PLA2 activity of Daboxin P by butein, mimosine and bakuchiol. International Journal of Biological Macromolecules, 165(Pt A), 1066–1078. https://doi.org/10.1016/j.ijbiomac.2020.09.223
   PubMedGoogle Scholar
• Dileep, K. V., Tintu, I., & Sadasivan, C. (2011). Molecular docking studies of curcumin analogs with phospholipase A2. Interdisciplinary Sciences, Computational Life Sciences, 3(3), 189–197. https://doi.org/10.1007/s12539-011-0090-9
   PubMed Web of Science ®Google Scholar
• Dos Santos, J. I., Cintra-Francischinelli, M., Borges, R. J., Fernandes, C. A. H., Pizzo, P., Cintra, A. C. O., Braz, A. S. K., Soares, A. M., & Fontes, M. R. M. (2011). Structural, functional, and bioinformatics studies reveal a new snake venom homologue phospholipase A 2 class. Proteins, 79(1), 61–78. https://doi.org/10.1002/prot.22858
   PubMed Web of Science ®Google Scholar
• Eberhardt, J., Santos-Martins, D., Tillack, A. F., & Forli, S. (2021). AutoDock Vina 1.2.0: New docking methods, expanded force field, and python bindings. Journal of Chemical Information and Modeling, 61(8), 3891–3898. https://doi.org/10.1021/acs.jcim.1c00203
   PubMed Web of Science ®Google Scholar
• Fan, H. W., & Monteiro, W. M. (2018). History and perspectives on how to ensure antivenom accessibility in the most remote areas in Brazil. Toxicon : official Journal of the International Society on Toxinology, 151, 15–23. https://doi.org/10.1016/j.toxicon.2018.06.070
   PubMed Web of Science ®Google Scholar
• Fernandes, C. A. H., Borges, R. J., Lomonte, B., & Fontes, M. R. M. (2014). A structure-based proposal for a comprehensive myotoxic mechanism of phospholipase A2-like proteins from viperid snake venoms. Biochimica Et Biophysica Acta, 1844(12), 2265–2276. https://doi.org/10.1016/j.bbapap.2014.09.015
   PubMed Web of Science ®Google Scholar
• Ferreira, S. d S., Silva, D. P. d., Torres-Rêgo, M., Silva-Júnior, A. A. d., & Fernandes-Pedrosa, M. d F. (2022). The potential of phenolic acids in therapy against snakebites: A review. Toxicon: official Journal of the International Society on Toxinology, 208(December 2021), 1–12. https://doi.org/10.1016/j.toxicon.2021.12.019
   PubMedGoogle Scholar
• Gomes, A. A. S., Cardoso, F. F., Souza, M. F., Oliveira, C. L. P., Perahia, D., Magro, A. J., & Fontes, M. R. M. (2020). The allosteric activation mechanism of a phospholipase A2-like toxin from Bothrops jararacussu venom: A dynamic description. Scientific Reports, 10(1), 1–15. https://doi.org/10.1038/s41598-020-73134-9
   PubMed Web of Science ®Google Scholar
• Gomes Heleno, M. A., Baldasso, P. A., Ponce-Soto, L. A., & Marangoni, S. (2013). Biochemical characterization and pharmacological properties of new basic PLABrTX-I isolated from Bothrops roedingeri (Roedinger’s Lancehead) mertens, 1942, snake venom. BioMed Research International, 2013, 591470. https://doi.org/10.1155/2013/591470
   PubMed Web of Science ®Google Scholar
• Gómez-Betancur, I., Gogineni, V., Salazar-Ospina, A., & León, F. (2019). Perspective on the therapeutics of anti-snake venom. Molecules, 24(18), 3276. https://doi.org/10.3390/molecules24183276
   PubMed Web of Science ®Google Scholar
• Gordon, J. C., Myers, J. B., Folta, T., Shoja, V., Heath, L. S., & Onufriev, A. (2005). H++: A server for estimating pKas and adding missing hydrogens to macromolecules. Nucleic Acids Research, 33(Web Server), W368–W371. https://doi.org/10.1093/nar/gki464
   PubMed Web of Science ®Google Scholar
• Guex, N., Peitsch, M. C., & Schwede, T. (2009). Automated comparative protein structure modeling with SWISS-MODEL and Swiss-PdbViewer: A historical perspective. Electrophoresis, 30(S1), S162–S173. https://doi.org/10.1002/elps.200900140
   PubMed Web of Science ®Google Scholar
• Gutiérrez, J. M., Albulescu, L. O., Clare, R. H., Casewell, N. R., Abd El-Aziz, T. M., Escalante, T., & Rucavado, A. (2021). The search for natural and synthetic inhibitors that would complement antivenoms as therapeutics for snakebite envenoming. Toxins, 13(7), 451. https://doi.org/10.3390/toxins13070451
   PubMed Web of Science ®Google Scholar
• Gutiérrez, J. M., Calvete, J. J., Habib, A. G., Harrison, R. A., Williams, D. J., & Warrell, D. A. (2017). Snakebite envenoming. Nature Reviews. Disease Primers, 3(1), 17063-17084. https://doi.org/10.1038/nrdp.2017.63
   Google Scholar
• Gutiérrez, J. M., León, G., & Lomonte, B. (2003). Pharmacokinetic-pharmacodynamic relationships of immunoglobulin therapy for envenomation. Clinical Pharmacokinetics, 42(8), 721–741. https://doi.org/10.2165/00003088-200342080-00002
   PubMed Web of Science ®Google Scholar
• Hess, B., Bekker, H., Berendsen, H. J. C., & Fraaije, J. G. E. M. (1997). LINCS: A Linear Constraint Solver for molecular simulations. Journal of Computational Chemistry, 18(12), 1463–1472. https://doi.org/10.1002/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H
   Web of Science ®Google Scholar
• Huancahuire-Vega, S., Ponce-Soto, L. A., Martins-de-Souza, D., & Marangoni, S. (2009). Structural and functional characterization of brazilitoxins II and III (BbTX-II and -III), two myotoxins from the venom of Bothrops brazili snake. Toxicon : official Journal of the International Society on Toxinology, 54(6), 818–827. https://doi.org/10.1016/j.toxicon.2009.06.008
   PubMed Web of Science ®Google Scholar
• Jakalian, A., Jack, D. B., & Bayly, C. I. (2002). Fast, efficient generation of high-quality atomic charges. AM1-BCC model: II. Parameterization and validation. Journal of Computational Chemistry, 23(16), 1623–1641. https://doi.org/10.1002/jcc.10128
   PubMed Web of Science ®Google Scholar
• Kasturiratne, A., Wickremasinghe, A. R., De Silva, N., Gunawardena, N. K., Pathmeswaran, A., Premaratna, R., Savioli, L., Lalloo, D. G., & De Silva, H. J. (2008). The global burden of snakebite: A literature analysis and modelling based on regional estimates of envenoming and deaths. PLoS Medicine, 5(11), e218. https://doi.org/10.1371/journal.pmed.0050218
   PubMed Web of Science ®Google Scholar
• Knudsen, C., & Laustsen, A. H. (2018). Recent advances in next generation snakebite antivenoms. Tropical Medicine and Infectious Disease, 3(2), 42. https://doi.org/10.3390/tropicalmed3020042
   PubMedGoogle Scholar
• Kortemme, T., Kim, D. E., & Baker, D. (2004). Computational alanine scanning of protein-protein interfaces. Science’s STKE, 2004(219), pl2. https://doi.org/10.1126/stke.2192004pl2
   PubMedGoogle Scholar
• Kumar, M. S., Amjesh, R., Bhaskaran, S., Delphin, R. D., Nair, A. S., & Sudhakaran, P. R. (2019). Molecular docking and dynamic studies of crepiside E beta glucopyranoside as an inhibitor of snake venom PLA2. Journal of Molecular Modeling, 25(4), 88-99. https://doi.org/10.1007/s00894-019-3954-2
   Web of Science ®Google Scholar
• Kumari, R., Kumar, R., Consortium, O. S. D. D., & Lynn, A. (2014). g _ mmpbsa – A GROMACS tool for MM-PBSA and its optimization for high-throughput binding energy calculations. Journal of Chemical Information and Modeling, 54(7), 1951–1962. https://doi.org/10.1021/ci500020m
   PubMed Web of Science ®Google Scholar
• Laustsen, A. H., Lohse, B., Lomonte, B., Engmark, M., & Gutiérrez, J. M. (2015). Selecting key toxins for focused development of elapid snake antivenoms and inhibitors guided by a Toxicity Score. Toxicon: Official Journal of the International Society on Toxinology, 104, 43–45. https://doi.org/10.1016/j.toxicon.2015.07.334
   PubMed Web of Science ®Google Scholar
• Lindorff-Larsen, K., Piana, S., Palmo, K., Maragakis, P., Klepeis, J. L., Dror, R. O., & Shaw, D. E. (2010). Improved side-chain torsion potentials for the Amber ff99SB protein force field. Proteins: Structure, Function, and Bioinformatics, 78(8), 1950–1958. https://doi.org/10.1002/prot.22711
   PubMed Web of Science ®Google Scholar
• Liu, Y., Staerk, D., Nielsen, M. N., Nyberg, N., & Jäger, A. K. (2015). High-resolution hyaluronidase inhibition profiling combined with HPLC–HRMS–SPE–NMR for identification of anti-necrosis constituents in Chinese plants used to treat snakebite. Phytochemistry, 119, 62–69. https://doi.org/10.1016/j.phytochem.2015.09.005
   PubMed Web of Science ®Google Scholar
• Mahmud, S., Parves, M. R., Riza, Y. M., Sujon, K. M., Ray, S., Tithi, F. A., Zaoti, Z. F., Alam, S., & Absar, N. (2020). Exploring the potent inhibitors and binding modes of phospholipase A2 through in silico investigation. Journal of Biomolecular Structure & Dynamics, 38(14), 4221–4231. https://doi.org/10.1080/07391102.2019.1680440
   PubMed Web of Science ®Google Scholar
• Marinetti, G. V. (1965). The action of phospholipase A on lipoproteins. Biochimica Et Biophysica Acta, 98(3), 554–565. https://doi.org/10.1016/0005-2760(65)90152-9
   PubMedGoogle Scholar
• Meza, J. C. (2010). Steepest descent. WIREs Computational Statistics, 2(6), 719–722. https://doi.org/10.1002/wics.117
   Google Scholar
• Montecucco, C., Gutiérrez, J. M., & Lomonte, B. (2008). Cellular pathology induced by snake venom phospholipase A2 myotoxins and neurotoxins: Common aspects of their mechanisms of action. Cellular and Molecular Life Sciences, 65(18), 2897–2912. https://doi.org/10.1007/s00018-008-8113-3
   PubMed Web of Science ®Google Scholar
• Muthusamy, K., Chinnasamy, S., Nagarajan, S., & Sivaraman, T. (2018). Computational and in vitro insights on snake venom phospholipase A(2) inhibitor of phytocompound ikshusterol3-O-glucoside of Clematis gouriana Roxb. ex DC. Journal of Biomolecular Structure & Dynamics, 36(16), 4197–4208. https://doi.org/10.1080/07391102.2017.1409653
   PubMed Web of Science ®Google Scholar
• Oleg, T., & Arthur, J. O. (2010). AutoDock vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. Journal of Computational Chemistry, 31(2), 455-461. https://doi.org/10.1002/jcc
   Web of Science ®Google Scholar
• Oliveira, A., Bleicher, L., Schrago, C. G., & Silva Junior, F. P. (2018). Conservation analysis and decomposition of residue correlation networks in the phospholipase A2 superfamily (PLA2s): Insights into the structure-function relationships of snake venom toxins. Toxicon : official Journal of the International Society on Toxinology, 146, 50–60. https://doi.org/10.1016/j.toxicon.2018.03.013
   PubMed Web of Science ®Google Scholar
• Renetseder, R., Brunie, S., Dijkstra, B. W., Drenth, J., & Sigler, P. B. (1985). A comparison of the crystal structures of phospholipase A2 from bovine pancreas and Crotalus atrox venom. The Journal of Biological Chemistry, 260(21), 11627–11634. https://doi.org/10.1016/S0021-9258(17)39077-4
   PubMed Web of Science ®Google Scholar
• Rodrigues, C. R., Molina, D. A. M., Silva de Assis, T. C., Liberato, C., Melo-Braga, M. N., Ferreyra, C. B., Cárdenas, J., Costal-Oliveira, F., Guerra-Duarte, C., & Chávez-Olórtegui, C. (2020). Proteomic and toxinological characterization of Peruvian pitviper Bothrops brazili (“jergón shushupe”), venom. Toxicon : official Journal of the International Society on Toxinology, 184(February), 19–27. https://doi.org/10.1016/j.toxicon.2020.05.016
   PubMedGoogle Scholar
• Salentin, S., Schreiber, S., Haupt, V. J., Adasme, M. F., & Schroeder, M. (2015). PLIP: Fully automated protein-ligand interaction profiler. Nucleic Acids Research, 43(W1), W443–W447. https://doi.org/10.1093/nar/gkv315
   PubMed Web of Science ®Google Scholar
• Salvador, G. H. M., Cardoso, F. F., Gomes, A. A., Cavalcante, W. L. G., Gallacci, M., & Fontes, M. R. M. (2019). Search for efficient inhibitors of myotoxic activity induced by ophidian phospholipase A 2 -like proteins using functional, structural and bioinformatics approaches. Scientific Reports, 9(1), 510-523. https://doi.org/10.1038/s41598-018-36839-6
   Google Scholar
• Salvador, G. H. M., Gomes, A. A. S., Bryan-Quirós, W., Fernández, J., Lewin, M. R., Gutiérrez, J. M., Lomonte, B., & Fontes, M. R. M. (2019). Structural basis for phospholipase A2-like toxin inhibition by the synthetic compound Varespladib (LY315920). Scientific Reports, 9(1), 1–13. https://doi.org/10.1038/s41598-019-53755-5
   PubMedGoogle Scholar
• Salvador, G. H. M., Pinto, Ê. K. R., Ortolani, P. L., Fortes-Dias, C. L., Cavalcante, W. L. G., Soares, A. M., Lomonte, B., Lewin, M. R., & Fontes, M. R. M. (2023). Structural basis of the myotoxic inhibition of the Bothrops pirajai PrTX-I by the synthetic varespladib. Biochimie, 207, 1–10. https://doi.org/10.1016/j.biochi.2022.11.006
   PubMed Web of Science ®Google Scholar
• Sanz, L., Pérez, A., Quesada-Bernat, S., Diniz-Sousa, R., Calderón, L. A., Soares, A. M., Calvete, J. J., & Caldeira, C. A. S. (2020). Venomics and antivenomics of the poorly studied Brazil’s lancehead, Bothrops brazili (Hoge, 1954), from the Brazilian State of Pará. Journal of Venomous Animals and Toxins Including Tropical Diseases, 26(February), 1–14. https://doi.org/10.1590/1678-9199-jvatitd-2019-0103
   Google Scholar
• Schaloske, R. H., & Dennis, E. A. (2006). The phospholipase A2 superfamily and its group numbering system. Biochimica et Biophysica Acta, 1761(11), 1246–1259. https://doi.org/10.1016/j.bbalip.2006.07.011
   PubMed Web of Science ®Google Scholar
• Sharifpour, S., Fakhraee, S., & Behjatmanesh-Ardakani, R. (2020). Insights into the mechanism of inhibition of phospholipase A2 by resveratrol: An extensive molecular dynamics simulation and binding free energy calculation. Journal of Molecular Graphics & Modelling, 100, 107649. https://doi.org/10.1016/j.jmgm.2020.107649
   PubMed Web of Science ®Google Scholar
• Silva, D. P. d., Ferreira, S. d S., Torres-Rêgo, M., Furtado, A. A., Yamashita, F. d O., Diniz, E. A. d S., Vieira, D. S., Ururahy, M. A. G., Silva-Júnior, A. A. d., Luna, K. P. d O., & Fernandes-Pedrosa, M. d F. (2022). Antiophidic potential of chlorogenic acid and rosmarinic acid against Bothrops leucurus snake venom. Biomedicine & Pharmacotherapy = Biomedecine & Pharmacotherapie, 148, 112766. https://doi.org/10.1016/j.biopha.2022.112766
   PubMed Web of Science ®Google Scholar
• Sousa Da Silva, A. W., & Vranken, W. F. (2012). ACPYPE – AnteChamber PYthon parser interfacE. BMC Research Notes, 5, 367. https://doi.org/10.1186/1756-0500-5-367
   PubMedGoogle Scholar
• Studer, G., Rempfer, C., Waterhouse, A. M., Gumienny, R., Haas, J., & Schwede, T. (2020). QMEANDisCo—Distance constraints applied on model quality estimation. Bioinformatics (Oxford, England), 36(6), 1765–1771. https://doi.org/10.1093/bioinformatics/btz828
   PubMed Web of Science ®Google Scholar
• Studer, G., Tauriello, G., Bienert, S., Biasini, M., Johner, N., & Schwede, T. (2021). ProMod3 - A versatile homology modelling toolbox. PLOS Computational Biology, 17(1), e1008667. https://doi.org/10.1371/journal.pcbi.1008667
   PubMed Web of Science ®Google Scholar
• Sucasaca-Monzón, G., Randazzo-Moura, P., Rocha, T., Torres-Huaco, F. D., Vilca-Quispe, A., Ponce-Soto, L. A., Marangoni, S., Da Cruz-Höfling, M. A., & Rodrigues-Simioni, L. (2015). Bp-13 PLA2: Purification and neuromuscular activity of a new Asp49 toxin isolated from bothrops pauloensis snake venom. Biochemistry Research International, 2015, 826059. https://doi.org/10.1155/2015/826059
   PubMedGoogle Scholar
• Tap, F. M., Abd Majid, F. A., Ismail, H. F., Wong, T. S., Shameli, K., Miyake, M., & Khairudin, N. B. A. (2018). In silico and in vitro study of the bromelain-phytochemical complex inhibition of phospholipase A2 (Pla2). Molecules, 23(1), 73. https://doi.org/10.3390/molecules23010073
   PubMed Web of Science ®Google Scholar
• Tasoulis, T., & Isbister, G. K. (2017). A review and database of snake venom proteomes. In Toxins, 9(9), 290. https://doi.org/10.3390/toxins9090290
   PubMed Web of Science ®Google Scholar
• Träg, J., & Zahn, D. (2019). Improved GAFF2 parameters for fluorinated alkanes and mixed hydro- and fluorocarbons. Journal of Molecular Modeling, 25(2), 39-48. https://doi.org/10.1007/s00894-018-3911-5
   Web of Science ®Google Scholar
• Turner, P. J. (2005). XMGRACE, Version 5.1. 19. Center for Coastal and Land-Margin Research, Oregon Graduate Institute of Science and Technology, 2.
   Google Scholar
• Van Gunsteren, W. F., & Berendsen, H. J. C. (1988). A leap-frog algorithm for stochastic dynamics. Molecular Simulation, 1(3), 173–185. https://doi.org/10.1080/08927028808080941
   Web of Science ®Google Scholar
• Vassetti, D., Pagliai, M., & Procacci, P. (2019). Assessment of GAFF2 and OPLS-AA general force fields in combination with the water models TIP3P, SPCE, and OPC3 for the solvation free energy of druglike organic molecules. Journal of Chemical Theory and Computation, 15(3), 1983–1995. https://doi.org/10.1021/acs.jctc.8b01039
   PubMed Web of Science ®Google Scholar
• Waskom, M. L. (2021). seaborn: Statistical data visualization. Journal of Open Source Software, 6(60), 3021. https://doi.org/10.21105/joss.03021
   Google Scholar
• Waterhouse, A., Bertoni, M., Bienert, S., Studer, G., Tauriello, G., Gumienny, R., Heer, F. T., de Beer, T. A. P., Rempfer, C., Bordoli, L., Lepore, R., & Schwede, T. (2018). SWISS-MODEL: Homology modelling of protein structures and complexes. Nucleic Acids Research, 46(W1), W296–W303. https://doi.org/10.1093/nar/gky427
   PubMed Web of Science ®Google Scholar
• Willard, L., Ranjan, A., Zhang, H., Zhang, H., Monzavi, H., Monzavi, H., Boyko, R. F., Boyko, R. F., Sykes, B. D., Sykes, B. D., Wishart, D. S., & Ds, W. (n.d). FAU FAU FAU FAU FAU VADAR: A web server for quantitative evaluation of protein structure quality. PG - 3316-9 (Issues 1362-4962 (Electronic)).
   Google Scholar
• World Health Assembly, 71. (n.d). Addressing the burden of snakebite envenoming. World Health Organization. https://apps.who.int/iris/handle/10665/279476
   Google Scholar
• WHO. (n.d). Snakebite envenoming: A strategy for prevention and control: Executive summary. World Health Organization. https://apps.who.int/iris/handle/10665/312195
   Google Scholar
• Xiao, H., Pan, H., Liao, K., Yang, M., & Huang, C. (2017). Snake venom PLA2, a promising target for broad-spectrum antivenom drug development. BioMed Research International, 2017, 6592820. https://doi.org/10.1155/2017/6592820
   PubMed Web of Science ®Google Scholar
• Yuan, S., Chan, H. C. S., & Hu, Z. (2017). Using PyMOL as a platform for computational drug design. WIREs Computational Molecular Science, 7(2), e1298. https://doi.org/10.1002/wcms.1298
   Google Scholar