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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

An Evaluation of 3-Rhamnosylquercetin, a Glycosylated Form of Quercetin, against the Myotoxic and Edematogenic Effects of sPLA(2) from Crotalus durissus terrificus

Texto completo
Autor(es):
Toyama, Daniela de Oliveira [1] ; Gaeta, Henrique Hessel [2] ; Terashima de Pinho, Marcus Vinicius [2, 3] ; Pena Ferreira, Marcelo Jose [4] ; Romoff, Paulete [4] ; Matioli, Fabio Filippi [5] ; Magro, Angelo Jose [5] ; de Mattos Fontes, Marcos Roberto [5] ; Toyama, Marcos Hikari [2]
Número total de Autores: 9
Afiliação do(s) autor(es):
[1] Univ Presbiteriana Mackenzie, CCBS, BR-01302907 Sao Paulo - Brazil
[2] UNESP, BIOMOLPEP, Lab Biol Mol & Peptideos, BR-11330900 Sao Vicente, SP - Brazil
[3] Univ Estadual Campinas, Fac Ciencias Med, Programa Posgrad Farmacol, BR-13083970 Campinas, SP - Brazil
[4] Univ Presbiteriana Mackenzie, Escola Engn, BR-01302907 Sao Paulo - Brazil
[5] UNESP, Inst Biociencias, Dept Fis & Biofis, BR-18618970 Botucatu, SP - Brazil
Número total de Afiliações: 5
Tipo de documento: Artigo Científico
Fonte: BIOMED RESEARCH INTERNATIONAL; 2014.
Citações Web of Science: 1
Resumo

This paper shows the results of quercitrin effects on the structure and biological activity of secretory phospholipase (sPLA(2)) from Crotalus durissus terrificus, which is the main toxin involved in the pharmacological effects of this snake venom. According to our mass spectrometry and circular dichroism results, quercetin was able to promote a chemical modification of some amino acid residues and modify the secondary structure of C. d. terrificus sPLA(2). Moreover, molecular docking studies showed that quercitrin can establish chemical interactions with some of the crucial amino acid residues involved in the enzymatic activity of the sPLA(2), indicating that this flavonoid could also physically impair substrate molecule access to the catalytic site of the toxin. Additionally, in vitro and in vivo assays showed that the quercitrin strongly diminished the catalytic activity of the protein, altered its Vmax and Km values, and presented a more potent inhibition of essential pharmacological activities in the C. d. terrificus sPLA(2), such as its myotoxicity and edematogenic effect, in comparison to quercetin. Thus, we concluded that the rhamnose group found in quercitrin is most likely essential to the antivenom activities of this flavonoid against C. d. terrificus sPLA(2). (AU)

Processo FAPESP: 13/12077-8 - Avaliação de extratos foliares de Laguncularia racemosa sobre atividade enzimática e farmacológica de fosfolipases A2 cataliticamente ativas de venenos
Beneficiário:Daniela de Oliveira Toyama
Linha de fomento: Auxílio à Pesquisa - Regular
Processo FAPESP: 11/06704-4 - Caracterização da atividade anti-fosfolipase A2 e avaliação do potencial anti-inflamatório de metabólitos especiais naturais e modificadas de plantas
Beneficiário:Marcos Hikari Toyama
Linha de fomento: Auxílio à Pesquisa - Regular
Processo FAPESP: 12/06502-5 - Estudos estruturais e funcionais com proteínas de veneno de serpentes nativas, recombinantes e complexadas com inibidores vegetais
Beneficiário:Marcos Roberto de Mattos Fontes
Linha de fomento: Auxílio à Pesquisa - Regular