Título :	Bowman-Birk protease inhibitor from Vigna unguiculata seeds enhances the action of bradykinin-related peptides
Autor :	Álvares, Alice da Cunha Morales Schwartz, Elisabeth Nogueira Ferroni Amaral, Nathalia Oda Trindade, Neidiane Rosa Pedrino, Gustavo Rodrigues Silva, Luciano Paulino Freitas, Sonia Maria de
Assunto::	Pressão arterial Bradicinina Espectroscopia
Fecha de publicación :	2014
Editorial :	MDPI
Citación :	ÁLVARES, Alice da Cunha Morales et al. Bowman-Birk protease inhibitor from Vigna unguiculata seeds enhances the action of bradykinin-related peptides. Molecules, v. 19, p. 17536-17558, 30 out. 2014. Disponível em: <http://www.mdpi.com/1420-3049/19/11/17536/htm>. Acesso em: 27 jul. 2017. doi: 10.3390/molecules191117536 .
Abstract:	The 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, Bk1 and Bk2, 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 103 to 104 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 Bk2 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.
Licença::	© 2014 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
DOI:	https://dx.doi.org/10.3390/molecules191117536
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