Made available in DSpace on 2013-09-27T14:53:09Z (GMT). No. of bitstreams: 1 WOS000287004200002.pdf: 811833 bytes, checksum: 8b39287f53b1d7f23d5aa49a1c231297 (MD5) Previous issue date: 2011-01-15 Made available in DSpace on 2013-09-30T17:41:37Z (GMT). No. of bitstreams: 1 WOS000287004200002.pdf: 811833 bytes, checksum: 8b39287f53b1d7f23d5aa49a1c231297 (MD5) Previous issue date: 2011-01-15 Submitted by Vitor Silverio Rodrigues (vitorsrodrigues@reitoria.unesp.br) on 2014-05-20T13:12:26Z No. of bitstreams: 1 WOS000287004200002.pdf: 811833 bytes, checksum: 8b39287f53b1d7f23d5aa49a1c231297 (MD5) Made available in DSpace on 2014-05-20T13:12:26Z (GMT). No. of bitstreams: 1 WOS000287004200002.pdf: 811833 bytes, checksum: 8b39287f53b1d7f23d5aa49a1c231297 (MD5) Previous issue date: 2011-01-15 Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) As polyphenolic compounds isolated from plants extracts, flavonoids have been applied to various pharmaceutical uses in recent decades due to their anti-inflammatory, cancer preventive, and cardiovascular protective activities. In this study, we evaluated the effects of the flavonoid quercetin on Crotalus durissus terrificus secretory phospholipase A2 (sPLA2), an important protein involved in the release of arachidonic acid from phospholipid membranes. The protein was chemically modified by treatment with quercetin, which resulted in modifications in the secondary structure as evidenced through circular dichroism. In addition, quercetin was able to inhibit the enzymatic activity and some pharmacological activities of sPLA2, including its antibacterial activity, its ability to induce platelet aggregation, and its myotoxicity by approximately 40%, but was not able to reduce the inflammatory and neurotoxic activities of sPLA2. These results suggest the existence of two pharmacological sites in the protein, one that is correlated with the enzymatic site and another that is distinct from it. We also performed molecular docking to better understand the possible interactions between quercetin and sPLA2. Our docking data showed the existence of hydrogen-bonded, polar interactions and hydrophobic interactions, suggesting that other flavonoids with similar structures could bind to sPLA2. Further research is warranted to investigate the potential use of flavonoids as sPLA2 inhibitors. (C) 2010 Elsevier B.V. All rights reserved. Univ Estadual Campinas, Inst Biol, Dept Bioquim, BR-13083862 Campinas, SP, Brazil Univ Estadual Campinas, Dept Farmacol, Fac Ciencias Med, Campinas, SP, Brazil Universidade Federal do Ceará (UFC), Lab Farm Venenos Toxinas & Lectinas LAFAVET, Dept Fisiol & Farmacol, Fortaleza, Ceara, Brazil Universidade Federal de Pernambuco (UFPE), LQTM, Dept Ciencias Farmaceut, Recife, PE, Brazil Univ Presbiteriana Mackenzie, CCBS, São Paulo, Brazil UNESP, Sao Vicente, SP, Brazil UNESP, Sao Vicente, SP, Brazil CNPq: 133151/2009-3