Interaction of proteinase inhibitors with phospholipid vesicles is modulated by pH

Interaction of proteinase inhibitors with phospholipid vesicles is modulated by pH

Author Silva-Lucca, Rosemeire A. Autor UNIFESP Google Scholar
Faneca, Henrique M. S. Google Scholar
Pedroso de Lima, Maria C. Google Scholar
De Caroli, Fernanda P. Autor UNIFESP Google Scholar
Assis, M. L. Autor UNIFESP Google Scholar
Sampaio, Misako U. Autor UNIFESP Google Scholar
Oliva, Maria Luiza V. Autor UNIFESP Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Univ Estadual Oeste Parana
Univ Coimbra
Abstract rBbKI and rBbCI, plant recombinant inhibitors from Bauhinia bauhinioides, and BpuTI from Bauhinia purpurea seeds distinctly and specifically block proteolytic enzymes. the secondary structures of those inhibitors were compared and their interactions with phospholipid vesicles were evaluated by the release of calcein and by intrinsic fluorescence of tryptophan residues. the results show that rBbKI, rBbCI and BpuTI are able to interact with phospholipd vesicles and induce membrane permeabilization in a concentration- and pH-dependent manner. the leakage was rapid and extensive at pH 4.5, but at physiological pH, no calcein release was observed. These results may suggest that upon inflammation or microorganism invasion accompanied by lowering of pH, appropriate conditions may occur for the inhibitors to interact with cell membrane and act on specific proteolytic enzyme. (C) 2010 Elsevier B.V. All rights reserved.
Keywords Bauhinia
Circular dichroism
Fluorescence spectroscopy
Liposome
Plant proteinase inhibitors
Phospholipid
Trypsin inhibitor
Language English
Sponsor Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Date 2010-11-01
Published in International Journal of Biological Macromolecules. Amsterdam: Elsevier B.V., v. 47, n. 4, p. 551-557, 2010.
ISSN 0141-8130 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 551-557
Origin http://dx.doi.org/10.1016/j.ijbiomac.2010.07.011
Access rights Closed access
Type Article
Web of Science ID WOS:000283007000020
URI http://repositorio.unifesp.br/handle/11600/33039

Show full item record




File

File Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)

Search


Browse

Statistics

My Account