Umbelliferone Induces Changes In The Structure And Pharmacological Activities Of Bn Iv, A Phospholipase A2 Isoform Isolated From Bothrops Neuwiedi

dc.creatorToyama D.D.O.
dc.creatorDiz Filho E.B.D.S.
dc.creatorCavada B.S.
dc.creatorda Rocha B.A.M.
dc.creatorde Oliveira S.C.B.
dc.creatorCotrim C.A.
dc.creatorSoares V.C.G.
dc.creatorDelatorre P.
dc.creatorMarangoni S.
dc.creatorToyama M.H.
dc.date2011
dc.date2015-06-30T20:32:27Z
dc.date2015-11-26T14:50:58Z
dc.date2015-06-30T20:32:27Z
dc.date2015-11-26T14:50:58Z
dc.date.accessioned2018-03-28T22:02:24Z
dc.date.available2018-03-28T22:02:24Z
dc.identifier
dc.identifierToxicon. , v. 57, n. 6, p. 851 - 860, 2011.
dc.identifier410101
dc.identifier10.1016/j.toxicon.2011.02.024
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-79954995046&partnerID=40&md5=ade795f6004ddad4afd62a6959409c74
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/108308
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/108308
dc.identifier2-s2.0-79954995046
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1254339
dc.descriptionIn this paper was demonstrated that umbelliferone induces changes in structure and pharmacological activities of Bn IV, a lysine 49 secretory phospholipase A2 (sPLA2) from Bothrops neuwiedi. Incubation of Bn IV with umbelliferone virtually abolished platelet aggregation, edema, and myotoxicity induced by native Bn IV. The amino acid sequence of Bn IV showed high sequence similarities with other Lys49 sPLA2s from B. jararacussu (BthTx-I), B. pirajai (PrTx-I), and B. neuwiedi pauloensis (Bn SP6 and Bn SP7). This sPLA2 also has a highly conserved C-terminal amino acid sequence, which has been shown as important for the pharmacological activities of Lys49 sPLA2. Sequencing of Bn IV previously treated with umbelliferone revealed modification of S(1) and S(20). Fluorescent spectral analysis and circular dichroism (CD) studies showed that umbelliferone modified the secondary structure of this protein. Moreover, the pharmacological activity of Bn IV is driven by synergism of the C-terminal region with the α-helix motifs, which are involved in substrate binding of the Asp49 and Lys49 residues of sPLA2 and have a direct effect on the Ca2+-independent membrane damage of some secretory snake venom PLA2. For Bn IV, these interactions are potentially important for triggering the pharmacological activity of this sPLA2. © 2011 Elsevier Ltd.
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dc.languageen
dc.publisher
dc.relationToxicon
dc.rightsfechado
dc.sourceScopus
dc.titleUmbelliferone Induces Changes In The Structure And Pharmacological Activities Of Bn Iv, A Phospholipase A2 Isoform Isolated From Bothrops Neuwiedi
dc.typeArtículos de revistas


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