Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/43446
Title: Bauhinia bauhinioides plasma kallikrein inhibitor: Interaction with synthetic peptides and fluorogenic peptide substrates related to the reactive site sequence
Authors: Oliva, Maria Luiza Vilela [UNIFESP]
Mendes, C. R.
Santomauro-Vaz, Eugenio Miguel [UNIFESP]
Juliano, Maria Aparecida [UNIFESP]
Mentele, R.
Auerswald, E. A.
Sampaio, Misako Uemura [UNIFESP]
Sampaio, Claudio Augusto Machado [UNIFESP]
Universidade Federal de São Paulo (UNIFESP)
LMU Munchen
Issue Date: 1-Jul-2001
Publisher: Bentham Science Publ Ltd
Citation: Current Medicinal Chemistry. Hilversum: Bentham Science Publ Ltd, v. 8, n. 8, p. 977-984, 2001.
Abstract: A serine proteinase inhibitor was purified from Bauhinia bauhinioides seeds after extraction with 0.15M NaCl by ion-exchange column chromatography on DEAE-Sephadex, gel filtration on Superose 12 column, Mono Q chromatography or alternatively by affinity chromatography on trypsin-Sepharose.The inhibitor is a single polypeptide chain with molecular mass 20 kDa by gel filtration on Superose 12; but was resolved into two peaks by ion-exchange chromatography on Mono Q (FPLC system). The main eluted peak inhibits trypsin (Ki=0.6 nM), plasma kallikrein (Ki=0.35 nM), plasmin (Ki=33.1 nM), and weakly chymotrypsin (Ki=2,700 nM), being the most effective plasma kallikrein inhibitor isolated from Bauhinia seeds. Therefore, it was denominated Bauhinia bauhinioides kallikrein inhibitor (BbKI). Activity is thermolabile and on trypsin inhibition optimum pH is 8.0.BbKI displays high homology to other plant Kunitz inhibitors, except for the absence of disulfide bridges, and the only cysteine residue is at the C-terminal position (residue 154) characterizes a distinct member of the Kunitz family. The affinity of the inhibitor to trypsin was confirmed by adsorption to trypsin-Sepharose resin and by isolation of the trypsin-inhibitor complex by gel filtration.Peptides with variations around the reactive site of BbKI (GLPVRFESPLRINIIKESY) were synthesized containing a quenched fluorogenic group. Trypsin but not plasma kallikrein substrates, these peptides strongly inhibited plasma kallikrein.
URI: http://repositorio.unifesp.br/11600/43446
ISSN: 0929-8673
Other Identifiers: http://dx.doi.org/10.2174/0929867013372779
Appears in Collections:Artigo
Artigo

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.