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Title: Bothrops moojeni myotoxin-II, a Lys49-phospholipase A2 homologue : an example of function versatility of snake venom proteins.
Authors: Stabeli, Rodrigo Guerino
Amui, Saulo França
Sant'Ana, Carolina Dalaqua
Pires, Matheus Godoy
Nomizo, Auro
Monteiro, Marta Chagas
Romão, Pedro Roosevelt Torres
Cota, Renata Guerra de Sá
Vieira, Carlos Alberto
Giglio, José Roberto
Fontes, Marcos Roberto de Mattos
Soares, Andreimar Martins
Keywords: Bothrops
Chemical modification
Issue Date: 2006
Citation: STABELI, R. G. et al. Bothrops moojeni myotoxin-II, a Lys49-phospholipase A2 homologue: an example of function versatility of snake venom proteins. Comparative Biochemistry and Physiology. C, Toxicology & Pharmacology, v. 142, p. 371-381, 2006. Disponível em: <>. Acesso em: 08 nov. 2014.
Abstract: MjTX-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.
ISSN: 1532-0456
metadata.dc.rights.license: O periódico Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology concede permissão para depósito deste artigo no Repositório Institucional da UFOP. Número da licença: 3547120459813.
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