Interaction of proteinase inhibitors with phospholipid vesicles is modulated by pH

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dc.contributor.authorSilva-Lucca, Rosemeire A. [UNIFESP]
dc.contributor.authorFaneca, Henrique M. S.
dc.contributor.authorPedroso de Lima, Maria C.
dc.contributor.authorDe Caroli, Fernanda P. [UNIFESP]
dc.contributor.authorAssis, M. L. [UNIFESP]
dc.contributor.authorSampaio, Misako U. [UNIFESP]
dc.contributor.authorOliva, Maria Luiza V. [UNIFESP]
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniv Estadual Oeste Parana
dc.contributor.institutionUniv Coimbra
dc.date.accessioned2016-01-24T14:05:38Z
dc.date.available2016-01-24T14:05:38Z
dc.date.issued2010-11-01
dc.description.abstractrBbKI 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.en
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniv Estadual Oeste Parana, Ctr Engn & Ciencias Exatas, BR-85903000 Toledo, PR, Brazil
dc.description.affiliationUniv Coimbra, Fac Ciencias & Tecnol, Ctr Neurociencias & Biol Celular, Dept Ciencias Vida, P-3001401 Coimbra, Portugal
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.format.extent551-557
dc.identifierhttp://dx.doi.org/10.1016/j.ijbiomac.2010.07.011
dc.identifier.citationInternational Journal of Biological Macromolecules. Amsterdam: Elsevier B.V., v. 47, n. 4, p. 551-557, 2010.
dc.identifier.doi10.1016/j.ijbiomac.2010.07.011
dc.identifier.issn0141-8130
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/33039
dc.identifier.wosWOS:000283007000020
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofInternational Journal of Biological Macromolecules
dc.rightsAcesso restrito
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectBauhiniaen
dc.subjectCircular dichroismen
dc.subjectFluorescence spectroscopyen
dc.subjectLiposomeen
dc.subjectPlant proteinase inhibitorsen
dc.subjectPhospholipiden
dc.subjectTrypsin inhibitoren
dc.titleInteraction of proteinase inhibitors with phospholipid vesicles is modulated by pHen
dc.typeArtigo
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