Citation

Gimenez GS, Coutinho-Neto A, Kayano AM, Simões-Silva R, Trindade F, de Almeida E Silva A, Marcussi S, da Silva SL, Fernandes CF, Zuliani JP, Calderon LA, Soares AM, Stábeli RG. Biomed. Res. Int. 2014; 2014: e950538.

Affiliation

Centro de Estudos de Biomoléculas Aplicadas a Saúde, CEBio, Fundação Oswaldo Cruz, Fiocruz Rondônia e Departamento de Medicina, Universidade Federal de Rondônia, UNIR, 76812-245 Porto Velho, RO, Brazil.

Copyright

(Copyright © 2014, Hindawi Publishing)

DOI

10.1155/2014/950538

PMID

24895632

Abstract

Toxins purified from the venom of spiders have high potential to be studied pharmacologically and biochemically. These biomolecules may have biotechnological and therapeutic applications. This study aimed to evaluate the protein content of Parawixia bistriata venom and functionally characterize its proteins that have potential for biotechnological applications. The crude venom showed no phospholipase, hemorrhagic, or anti-Leishmania activities attesting to low genotoxicity and discrete antifungal activity for C. albicans. However the following activities were observed: anticoagulation, edema, myotoxicity and proteolysis on casein, azo-collagen, and fibrinogen. The chromatographic and electrophoretic profiles of the proteins revealed a predominance of acidic, neutral, and polar proteins, highlighting the presence of proteins with high molecular masses. Five fractions were collected using cation exchange chromatography, with the P4 fraction standing out as that of the highest purity. All fractions showed proteolytic activity. The crude venom and fractions P1, P2, and P3 showed larvicidal effects on A. aegypti. Fraction P4 showed the presence of a possible metalloprotease (60 kDa) that has high proteolytic activity on azo-collagen and was inhibited by EDTA. The results presented in this study demonstrate the presence of proteins in the venom of P. bistriata with potential for biotechnological applications.

Language: en