Structure of cruzipain/cruzain inhibitors isolated from Bauhinia bauhinioides seeds

Structure of cruzipain/cruzain inhibitors isolated from Bauhinia bauhinioides seeds

Author Oliveira, Cleide de Autor UNIFESP Google Scholar
Santana, Lucimeire Aparecida de Autor UNIFESP Google Scholar
Carmona, Adriana Karaoglanovic Autor UNIFESP Google Scholar
Cezari, Maria Helena Sedenho Autor UNIFESP Google Scholar
Sampaio, Misako Uemura Autor UNIFESP Google Scholar
Sampaio, Claudio Augusto Machado Autor UNIFESP Google Scholar
Oliva, Maria Luiza Vilela Autor UNIFESP Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Abstract The saline extract of Bauhinia bauhinioides dry seeds was shown to inhibit cruzipain, a cysteine proteinase from Trypanosoma cruzi. The inhibitory activity was assigned to a protein with 164 amino acid residues and molecular mass of 18 034 Da that was purified by chromatography on DEAE-Sephadex, trypsin-Sepharose (removal of trypsin inhibitors), Mono Q and a reversed-phase C-4 column. The primary structure is homologous to other plant Kunitz-type inhibitors, but it lacks cysteine residues and therefore the disulfide bridges. No methionine residue was identified by amino acid sequencing.The inhibition of cruzipain fits into a slow-tight binding mechanism with a low dissociation constant (K-i 1.2 nM). The studied Bauhinia protein also inhibits cruzain (K-i 0.3 nM), a C-terminally truncated recombinant species of cruzipain. Cathepsin L, a cysteine proteinase with high homology to cruzipain, is also inhibited (K-i 0.22 nM), but not cathepsin B, papain, bromelain or ficin.
Keywords cathepsin
cysteine proteinase inhibitor
Trypanosoma cruzi
Language English
Date 2001-05-01
Published in Biological Chemistry. Berlin: Walter De Gruyter & Co, v. 382, n. 5, p. 847-852, 2001.
ISSN 1431-6730 (Sherpa/Romeo, impact factor)
Publisher Walter De Gruyter & Co
Extent 847-852
Access rights Closed access
Type Article
Web of Science ID WOS:000169893300018

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