Action of Bauhinia bauhinioides synthetic peptides on serine proteinases.

Abstract:

:The kallikrein inhibitor found in Bauhinia bauhinioides seeds (BbKI) differs from classical Kunitz plant inhibitors in the lack of disulfide bridges in its structure [Biochim. Biophys. Acta 1477 (2000) 64-74]. In this study, we examined whether structural properties may be involved in inhibitory specificity and, if so, whether those properties might be useful tools in designing compounds that interfere with enzyme activity. Peptides structurally related to the BbKI (RPGLPVRFESPLRINIIKE-NH(2)) reactive site were synthesized by solid-phase method and assayed for serine proteinase activity. The peptides RPGLPVRFESPLRINIIKE-NH(2), RPGLPVRFESPL-NH(2), and GLPVRFES-NH(2) were efficient tissue kallikrein inhibitors, with I(50) values of 0.54 microM, 0.87 microM, and 0.5mM, respectively. The lasting inhibitory effect was observed in incubation periods of up to 120 min. None of the studied peptides interfere with the activity of thrombin, factor Xa or trypsin, although the native protein BbKI is a potent trypsin inhibitor.

authors

Cagliari CI,De Caroli FP,Nakahata AM,Araújo MS,Nakaie CR,Sampaio MU,Sampaio CA,Oliva ML

doi

10.1016/j.bbrc.2003.09.203

subject

Has Abstract

pub_date

2003-11-07 00:00:00

pages

241-5

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006291X03020527

journal_volume

311

pub_type

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