Bothrops moojeni myotoxin-II, a Lys49-phospholipase A2 homologue : an example of function versatility of snake venom proteins.

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Autor(es): dc.creatorStabeli, Rodrigo Guerino-
Autor(es): dc.creatorAmui, Saulo França-
Autor(es): dc.creatorSant'Ana, Carolina Dalaqua-
Autor(es): dc.creatorPires, Matheus Godoy-
Autor(es): dc.creatorNomizo, Auro-
Autor(es): dc.creatorMonteiro, Marta Chagas-
Autor(es): dc.creatorRomão, Pedro Roosevelt Torres-
Autor(es): dc.creatorCota, Renata Guerra de Sá-
Autor(es): dc.creatorVieira, Carlos Alberto-
Autor(es): dc.creatorGiglio, José Roberto-
Autor(es): dc.creatorFontes, Marcos Roberto de Mattos-
Autor(es): dc.creatorSoares, Andreimar Martins-
Data de aceite: dc.date.accessioned2025-08-21T16:01:29Z-
Data de disponibilização: dc.date.available2025-08-21T16:01:29Z-
Data de envio: dc.date.issued2015-03-06-
Data de envio: dc.date.issued2015-03-06-
Data de envio: dc.date.issued2006-
Fonte completa do material: dc.identifierhttp://www.repositorio.ufop.br/handle/123456789/4553-
Fonte completa do material: dc.identifierhttps://doi.org/10.1016/j.cbpc.2005.11.020-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1030249-
Descrição: dc.descriptionMjTX-II, a myotoxic phospholipase A2 (PLA2) homologue from Bothrops moojeni venom, was functionally and structurally characterized. The MjTX-II characterization included: (i) functional characterization (antitumoral, antimicrobial and antiparasitic effects); (ii) effects of structural modifications by 4-bromophenacyl bromide (BPB), cyanogen bromide (CNBr), acetic anhydride and 2-nitrobenzenesulphonyl fluoride (NBSF); (iii) enzymatic characterization: inhibition by low molecular weight heparin and EDTA; and (iv) molecular characterization: cDNA sequence and molecular structure prediction. The results demonstrated that MjTX-II displayed antimicrobial activity by growth inhibition against Escherichia coli and Candida albicans, antitumoral activity against Erlich ascitic tumor (EAT), human breast adenocarcinoma (SK-BR-3) and human T leukemia cells (JURKAT) and antiparasitic effects against Schistosoma mansoni and Leishmania spp., which makes MjTX-II a promising molecular model for future therapeutic applications, as well as other multifunctional homologous Lys49-PLA2s or even derived peptides. This work provides useful insights into the structural determinants of the action of Lys49-PLA2 homologues and, together with additional strategies, supports the concept of the presence of others “bioactive sites” distinct from the catalytic site in snake venom myotoxic PLA2s.-
Formato: dc.formatapplication/pdf-
Idioma: dc.languageen-
Direitos: dc.rightsO periódico Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology concede permissão para depósito deste artigo no Repositório Institucional da UFOP. Número da licença: 3547120459813.-
Palavras-chave: dc.subjectBothrops-
Palavras-chave: dc.subjectChemical modification-
Palavras-chave: dc.subjectMyotoxin-
Palavras-chave: dc.subjectMicrobial-
Palavras-chave: dc.subjectPhospholipase-
Título: dc.titleBothrops moojeni myotoxin-II, a Lys49-phospholipase A2 homologue : an example of function versatility of snake venom proteins.-
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