An evaluation of 3-rhamnosylquertetin, a glycolylated form of quercitin, against the myotoxic and edematogenic effects of sPLA2s from Crotalus durissus terrificus

dc.contributorUniversidade Presbiteriana Mackenzie
dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade Estadual de Campinas (UNICAMP)
dc.creatorToyama, Daniela de Oliveira
dc.creatorGaeta, Henrique Hessel [UNESP]
dc.creatorPinho, Marcus Vinícius Terashima de [UNESP]
dc.creatorFerreira, Marcelo José Pena [UNESP]
dc.creatorRomoff, Paulete
dc.creatorMatioli, Fábio Filippi [UNESP]
dc.creatorMagro, Angelo José [UNESP]
dc.creatorFontes, Marcos Roberto de Mattos [UNESP]
dc.creatorToyama, Marcos Hikari [UNESP]
dc.date2016-04-01T18:45:10Z
dc.date2016-04-01T18:45:10Z
dc.date2014
dc.date.accessioned2023-09-12T09:17:45Z
dc.date.available2023-09-12T09:17:45Z
dc.identifierhttp://dx.doi.org/10.1155/2014/341270
dc.identifierJournal of Biomedicine and Biotechnology, v. 2014, p. 1-11, 2014.
dc.identifier1110-7243
dc.identifierhttp://hdl.handle.net/11449/137317
dc.identifier10.1155/2014/341270
dc.identifierISSN1110-7243-2014-2014-01-11.pdf
dc.identifier8573195327542061
dc.identifier4320362411241786
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8786556
dc.descriptionThis paper shows the results of quercitrin effects on the structure and biological activity of secretory phospholipase (sPLA2) 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 sPLA2. 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 sPLA2, 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 sPLA2, 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 sPLA2.
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionInstituto Nacional para Pesquisa em Toxinas (INCT-Tox)
dc.descriptionUniversidade Presbiteriana Mackenzie, Centro de Ciências Biológicas e da Saúde (CCBS), São Paulo, SP, Brasil
dc.descriptionUniversidade Estadual Paulista Júlio de Mesquita Filho (UNESP), Instituto de Biociências, Departamento de Ciências Biológicas, São Vicente, SP, Brasil
dc.descriptionUniversidade Estadual de Campinas (UNICAMP), Faculdade de Ciências Médicas, Campinas, SP, Brasil
dc.descriptionUniversidade Presbiteriana Mackenzie, Escola de Engenharia, São Paulo, SP, Brasil
dc.descriptionUniversidade Estadual Paulista Júlio de Mesquita Filho (UNESP), Instituto de Biociências de Botucatu (IBB), Departamento de Física e Biofísica, Botucatu, SP, Brasil
dc.descriptionUniversidade Estadual Paulista Júlio de Mesquita Filho (UNESP), Instituto de Biociências, Departamento de Ciências Biológicas, São Vicente, SP, Brasil
dc.descriptionUniversidade Estadual Paulista Júlio de Mesquita Filho (UNESP), Instituto de Biociências de Botucatu (IBB), Departamento de Física e Biofísica, Botucatu, SP, Brasil
dc.descriptionFAPESP: 2011/06704-4
dc.descriptionFAPESP: 2012/06502-5
dc.descriptionFAPESP: 2013/12077-8
dc.format1-11
dc.languageeng
dc.relationJournal of Biomedicine and Biotechnology
dc.rightsAcesso aberto
dc.sourceCurrículo Lattes
dc.titleAn evaluation of 3-rhamnosylquertetin, a glycolylated form of quercitin, against the myotoxic and edematogenic effects of sPLA2s from Crotalus durissus terrificus
dc.typeArtigo


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