Quercetin As An Inhibitor Of Snake Venom Secretory Phospholipase A2

dc.creatorCotrim C.A.
dc.creatorDe Oliveira S.C.B.
dc.creatorDiz Filho E.B.S.
dc.creatorFonseca F.V.
dc.creatorBaldissera Jr. L.
dc.creatorAntunes E.
dc.creatorXimenes R.M.
dc.creatorMonteiro H.S.A.
dc.creatorRabello M.M.
dc.creatorHernandes M.Z.
dc.creatorDe Oliveira Toyama D.
dc.creatorToyama M.H.
dc.date2011
dc.date2015-06-30T20:36:09Z
dc.date2015-11-26T14:51:57Z
dc.date2015-06-30T20:36:09Z
dc.date2015-11-26T14:51:57Z
dc.date.accessioned2018-03-28T22:03:50Z
dc.date.available2018-03-28T22:03:50Z
dc.identifier
dc.identifierChemico-biological Interactions. , v. 189, n. 01/02/15, p. 9 - 16, 2011.
dc.identifier92797
dc.identifier10.1016/j.cbi.2010.10.016
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-79251624606&partnerID=40&md5=aafec89dab700c84e3c9f1b3edb22472
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/108584
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/108584
dc.identifier2-s2.0-79251624606
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1254666
dc.descriptionAs 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. © 2010 Elsevier Ireland Ltd. All rights reserved.
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dc.description01/02/15
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dc.languageen
dc.publisher
dc.relationChemico-Biological Interactions
dc.rightsfechado
dc.sourceScopus
dc.titleQuercetin As An Inhibitor Of Snake Venom Secretory Phospholipase A2
dc.typeArtículos de revistas


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