Bowman-birk protease inhibitor from vigna unguiculata seeds enhances the action of bradykinin-related peptides
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Data
2014
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Resumo
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, 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.
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Arterial blood pressure, Fluorescence spectroscopy, Bradykinin, Bowman-Birk inhibitor, Circular dichroism, Dynamic light scattering
Citação
ALVARES, 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.