Biochemical and functional characterization of parawixia bistriata spider venom with potential proteolytic and larvicidal activities

dc.creatorGimenez, Gizeli S.
dc.creatorCoutinho-Neto, Antonio
dc.creatorKayano, Anderson M.
dc.creatorSilva, Rodrigo Simões
dc.creatorTrindade, Frances
dc.creatorSilva, Alexandre de Almeida e
dc.creatorMarcussi, Silvana
dc.creatorSilva, Saulo L. da
dc.creatorFernandes, Carla F. C.
dc.creatorZuliani, Juliana P.
dc.creatorCalderon, Leonardo A.
dc.creatorSoares, Andreimar M.
dc.creatorStábeli, Rodrigo G.
dc.date2016-05-16T21:12:26Z
dc.date2016-05-16T21:12:26Z
dc.date2014
dc.date.accessioned2023-09-26T20:21:41Z
dc.date.available2023-09-26T20:21:41Z
dc.identifierSOARES, A.M., et al. Biochemical and Functional Characterization of Parawixia bistriata Spider Venom with Potential Proteolytic and Larvicidal Activities. BioMed Research International, v. 2014, p. 1-13, 2014.
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/14300
dc.identifierhttp://dx.doi.org/10.1155/2014/950538
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8855121
dc.descriptionToxins 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.
dc.formatapplication/pdf
dc.languageeng
dc.publisherBioMed Research International
dc.rightsopen access
dc.subjectParawixia bistriata
dc.subjectSpider Venom
dc.subjectPotential Proteolytic
dc.subjectLarvicidal Activities
dc.titleBiochemical and functional characterization of parawixia bistriata spider venom with potential proteolytic and larvicidal activities
dc.typeArticle


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