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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 386, Issue 6

Issues

Kunitz-type Bauhinia bauhinioides inhibitors devoid of disulfide bridges: isolation of the cDNAs, heterologous expression and structural studies

Ana Paula Ulian Araújo
  • Instituto de Física de São Carlos, USP, Avenida Trabalhador Sãocarlense 400, 13560-970 São Carlos, SP, Brazil
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/ Daiane Hansen
  • Universidade Federal de São Paulo, Escola Paulista de Medicina, Rua Três de Maio 100, 04044-020 São Paulo, SP, Brazil
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/ Debora F. Vieira
  • Instituto de Física de São Carlos, USP, Avenida Trabalhador Sãocarlense 400, 13560-970 São Carlos, SP, Brazil
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/ Cleide de Oliveira
  • Universidade Federal de São Paulo, Escola Paulista de Medicina, Rua Três de Maio 100, 04044-020 São Paulo, SP, Brazil
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/ Lucimeire A. Santana
  • Universidade Federal de São Paulo, Escola Paulista de Medicina, Rua Três de Maio 100, 04044-020 São Paulo, SP, Brazil
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/ Leila M. Beltramini
  • Instituto de Física de São Carlos, USP, Avenida Trabalhador Sãocarlense 400, 13560-970 São Carlos, SP, Brazil
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/ Claudio A.M. Sampaio
  • Universidade Federal de São Paulo, Escola Paulista de Medicina, Rua Três de Maio 100, 04044-020 São Paulo, SP, Brazil
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/ Misako U. Sampaio
  • Universidade Federal de São Paulo, Escola Paulista de Medicina, Rua Três de Maio 100, 04044-020 São Paulo, SP, Brazil
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/ Maria Luiza V. Oliva
  • Universidade Federal de São Paulo, Escola Paulista de Medicina, Rua Três de Maio 100, 04044-020 São Paulo, SP, Brazil
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Published Online: 2005-07-07 | DOI: https://doi.org/10.1515/BC.2005.066

Abstract

Bauhinia bauhinoides cruzipain inhibitor (BbCI) and Bauhinia bauhinioides kallikrein inhibitor (BbKI) are cysteine and serine proteinase inhibitors structurally homologous to plant Kunitz-type inhibitors, but are devoid of disulfide bridges. Based on cDNA sequences, we found that BbKI and BbCI are initially synthesized as a prepropeptide comprising an N-terminal signal peptide (19 residues), the mature protein (164 residues) and a C-terminal targeting peptide (10 residues). Partial cDNAs encoding the mature enzymes plus N-terminal His-tags and thrombin cleavage sites were expressed in E. coli and the soluble proteins were purified by one-step nickel affinity chromatography. After thrombin cleavage, both proteins exhibited potent inhibitory activities toward their cognate proteinases like the wild-type proteins. BbCI inhibits human neutrophil elastase (K i(app) 5.3 nM), porcine pancreatic elastase (K i(app) 40 nM), cathepsin G (K i(app) 160 nM) and the cysteine proteinases cruzipain (K i(app) 1.2 nM), cruzain (K i(app) 0.3 nM) and cathepsin L (K i(app) 2.2 nM), while BbKI strongly inhibits plasma kallikrein (K i(app) 2.4 nM) and plasmin (K i(app) 33 nM). Circular dichroism spectra of BbCI and BbKI were in agreement with the β-trefoil fold described for Kunitz inhibitors. The inhibitory potency of both BbCI- and BbKI-type inhibitors suggests that other, non-covalent interactions may compensate for the lack of disulfide bridges.

Keywords: cathepsins; cruzipain; elastase; gene; kallikreins; proteinase inhibitors

About the article

Corresponding author


Received: February 3, 2005

Accepted: April 8, 2005

Published Online: 2005-07-07

Published in Print: 2005-06-01


Citation Information: Biological Chemistry, Volume 386, Issue 6, Pages 561–568, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2005.066.

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