Effects of oxidation of lysozyme by hypohalous acids and haloamines on enzymatic activity and aggregation

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dc.contributor.authorPetronio, Maicon S.
dc.contributor.authorXimenes, Valdecir Farias [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T13:23:52Z
dc.date.available2014-05-20T13:23:52Z
dc.date.issued2012-10-01
dc.description.abstractHen egg white lysozyme (HEL), an antibacterial enzyme, is a prototype protein for studying the physical and chemical events that underlie the formation of amyloid fibril aggregates. Here, we studied alterations in enzymatic activity and aggregation provoked by oxidation of HEL by hypochlorous acid (HOCI), hypobromous acid (HOBr), taurine chloramine (Tau-NHCI), taurine monobromamine (Tau-NHBr), and taurine dibromamine (Tau-NBr2). Addition of only 4-fold molar excess of Tau-NHBr or Tau-NBr2 to HEL caused complete depletion of its intrinsic fluorescence, whereas HOCI and HOBr caused 40%-50% bleaching. Tau-NHCI was unable to oxidize lysozyme. The selective effect of bromamines on tryptophan residues had a direct effect on enzymatic activity: bromamines were about two-fold more effective as inhibitors of lysozyme than the acid precursors. The oxidation of HEL by HOCI and HOBr was more effective regarding the aggregation of the protein, which was evidenced by increased turbidity, Rayleigh scattering, and anisotropy. The aggregates presented spectroscopic properties that suggested the formation of amyloid fibrils, as measured by the thioflavin assay. In conclusion, the capacity of Tau-NHBr and Tau-NBr2 as inhibitors of the bactericidal activity of HEL could represent a role in the exacerbation of pulmonary infection, since leukocytes are rich sources of both taurine and HOBr. Moreover, the oxidation of HEL by just a small excess of hypohalous acids, a condition that could be found in inflammatory sites, may represent a new pathway for initiation of aggregation. (C) 2012 Elsevier B.V. All rights reserved.en
dc.description.affiliationUnesp Univ Estadual Paulista, Fac Ciencias Farmaceut, Dept Anal Clin, Araraquara, SP, Brazil
dc.description.affiliationUnesp Univ Estadual Paulista, Fac Ciencias, Dept Quim, Bauru, SP, Brazil
dc.description.affiliationUnespUnesp Univ Estadual Paulista, Fac Ciencias Farmaceut, Dept Anal Clin, Araraquara, SP, Brazil
dc.description.affiliationUnespUnesp Univ Estadual Paulista, Fac Ciencias, Dept Quim, Bauru, SP, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent1090-1096
dc.identifierhttp://dx.doi.org/10.1016/j.bbapap.2012.06.013
dc.identifier.citationBiochimica Et Biophysica Acta-proteins and Proteomics. Amsterdam: Elsevier B.V., v. 1824, n. 10, p. 1090-1096, 2012.
dc.identifier.doi10.1016/j.bbapap.2012.06.013
dc.identifier.issn1570-9639
dc.identifier.lattes4066413997908572
dc.identifier.urihttp://hdl.handle.net/11449/7271
dc.identifier.wosWOS:000307918300003
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochimica et Biophysica Acta: Proteins and Proteomics
dc.relation.ispartofjcr2.609
dc.relation.ispartofsjr1,170
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectAmyloid fibrilen
dc.subjectLysozyme activityen
dc.subjectHypobromous aciden
dc.subjectHypochlorous aciden
dc.subjectTaurine monobromamineen
dc.subjectTaurine dibromamineen
dc.titleEffects of oxidation of lysozyme by hypohalous acids and haloamines on enzymatic activity and aggregationen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes4066413997908572
unesp.author.orcid0000-0003-2636-3080[2]
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Farmacêuticas, Araraquarapt
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências, Baurupt

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