Please use this identifier to cite or link to this item:
Title: Action of Bauhinia bauhinioides synthetic peptides on serine proteinases
Authors: Cagliari, C. I.
De Caroli, F. P.
Nakahata, A. M.
Araujo, M. S.
Nakaie, C. R.
Sampaio, M. U.
Sampaio, CAM
Oliva, MLV
Universidade Federal de São Paulo (UNIFESP)
Keywords: Bauhinia bauhinioides
Kunitz inhibitor
plant inhibitor
primary structure
serine proteinase
tissue kallikrein
Issue Date: 7-Nov-2003
Publisher: Elsevier B.V.
Citation: Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 311, n. 1, p. 241-245, 2003.
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-NH2) reactive site were synthesized by solid-phase method and assayed for serine proteinase activity. the peptides RPGLPVRFESPLRINIIKE-NH2, RPGLPVRFESPL-NH2, and GLPVRFES-NH2 were efficient tissue kallikrein inhibitors, with I-50 values of 0.54 muM, 0.87 muM, and 0.5 mM, 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. (C) 2003 Elsevier Inc. All rights reserved.
ISSN: 0006-291X
Other Identifiers:
Appears in Collections:Em verificação - Geral

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.