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dc.creatorÁlvares, Alice da Cunha Morales-
dc.creatorSchwartz, Elisabeth Nogueira Ferroni-
dc.creatorAmaral, Nathalia Oda-
dc.creatorTrindade, Neidiane Rosa-
dc.creatorPedrino, Gustavo Rodrigues-
dc.creatorSilva, Luciano Paulino-
dc.creatorFreitas, Sonia Maria de-
dc.date.accessioned2018-09-12T11:35:05Z-
dc.date.available2018-09-12T11:35:05Z-
dc.date.issued2014-
dc.identifier.citationALVARES, Alice da Cunha M. et al. Bowman-birk protease inhibitor from vigna unguiculata seeds enhances the action of bradykinin-related peptides. Molecules, Basel, v. 19, p. 17536-17558, 2014.pt_BR
dc.identifier.issn1420-3049-
dc.identifier.issne- 1420-3049-
dc.identifier.urihttp://repositorio.bc.ufg.br/handle/ri/15908-
dc.description.abstractThe hydrolysis of bradykinin (Bk) by different classes of proteases in plasma and tissues leads to a decrease in its half-life. Here, Bk actions on smooth muscle and in vivo cardiovascular assays in association with a protease inhibitor, Black eyed-pea trypsin and chymotrypsin inhibitor (BTCI) and also under the effect of trypsin and chymotrypsin were evaluated. Two synthetic Bk-related peptides, Bk 1 and Bk 2 , were used to investigate the importance of additional C-terminal amino acid residues on serine protease activity. BTCI forms complexes with Bk and analogues at pH 5.0, 7.4 and 9.0, presenting binding constants ranging from 10 3 to 10 4 M −1 . Formation of BTCI-Bk complexes is probably driven by hydrophobic forces, coupled with slight conformational changes in BTCI. In vitro assays using guinea pig (Cavia porcellus) ileum showed that Bk retains the ability to induce smooth muscle contraction in the presence of BTCI. Moreover, no alteration in the inhibitory activity of BTCI in complex with Bk and analogous was observed. When the BTCI and BTCI-Bk complexes were tested in vivo, a decrease of vascular resistance and consequent hypotension and potentiating renal and aortic vasodilatation induced by Bk and Bk 2 infusions was observed. These results indicate that BTCI-Bk complexes may be a reliable strategy to act as a carrier and protective approach for Bk-related peptides against plasma serine proteases cleavage, leading to an increase in their half-life. These findings also indicate that BTCI could remain stable in some tissues to inhibit chymotrypsin or trypsin-like enzymes that cleave and inactivate bradykinin in situ.pt_BR
dc.language.isoengpt_BR
dc.rightsAcesso Abertopt_BR
dc.subjectArterial blood pressurept_BR
dc.subjectFluorescence spectroscopypt_BR
dc.subjectBradykininpt_BR
dc.subjectBowman-Birk inhibitorpt_BR
dc.subjectCircular dichroismpt_BR
dc.subjectDynamic light scatteringpt_BR
dc.titleBowman-birk protease inhibitor from vigna unguiculata seeds enhances the action of bradykinin-related peptidespt_BR
dc.typeArtigopt_BR
dc.publisher.countrySuicapt_BR
dc.identifier.doi10.3390/molecules191117536-
dc.publisher.departmentInstituto de Ciências Biológicas - ICB (RG)pt_BR
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