Inhibition of lysozyme by taurine dibromamine

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorPetrônio, M. S.-
Autor(es): dc.creatorXimenes, V. F.-
Data de aceite: dc.date.accessioned2025-08-21T17:33:02Z-
Data de disponibilização: dc.date.available2025-08-21T17:33:02Z-
Data de envio: dc.date.issued2022-04-29-
Data de envio: dc.date.issued2022-04-29-
Data de envio: dc.date.issued2013-11-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.2174/0929866511320110007-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/227314-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/227314-
Descrição: dc.descriptionHypobromous acid (HOBr) is a powerful oxidant produced by stimulated neutrophils and eosinophils. Taurine, a non-protein amino acid present in high amounts in the leukocytes, reacts instantaneously with HOBr leading to their haloamine derivative taurine dibromamine (Tau-NBr2). Lysozyme is a bactericidal enzyme also present in leukocytes and in secretory fluids. The inhibition of lysozyme is a pathway for bacterial proliferation in inflammatory sites. Here, we investigated the inhibition of the enzymatic activity of lysozyme when it was submitted to oxidation by Tau-NBr2. We found that the oxidation of lysozyme by Tau-NBr2 decreased its enzymatic activity in 80%, which was significant higher compared to the effect of its precursor HOBr (30%). The study and comparison of Tau-NBr2 and HOBr regarding the alterations provoked in the intrinsic fluorescence, synchronous fluorescence, resonance light scattering and near and far-UV circular dichroism spectra of lysozyme and oxidized lysozyme revealed that tryptophan residues in the active site of the protein were the main target for Tau-NBr2 and could explain its efficacy as inhibitor of lysozyme enzymatic activity. This property of Tau-NBr2 may have pathological significance, since it can be easily produced in the inflammatory sites. © 2013 Bentham Science Publishers.-
Descrição: dc.descriptionDepartment of Chemistry Faculty of Sciences São Paulo State University (UNESP), 17033-360, Bauru, São Paulo-
Descrição: dc.descriptionDepartment of Clinical Analysis School of Pharmaceutical Sciences São Paulo State University (UNESP), 14801-902, Araraquara, São Paulo-
Descrição: dc.descriptionDepartment of Chemistry Faculty of Sciences São Paulo State University (UNESP), 17033-360, Bauru, São Paulo-
Descrição: dc.descriptionDepartment of Clinical Analysis School of Pharmaceutical Sciences São Paulo State University (UNESP), 14801-902, Araraquara, São Paulo-
Formato: dc.format1232-1237-
Idioma: dc.languageen-
Relação: dc.relationProtein and Peptide Letters-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectEosinophils-
Palavras-chave: dc.subjectHypobromous acid-
Palavras-chave: dc.subjectHypochlorous acid-
Palavras-chave: dc.subjectLysozyme-
Palavras-chave: dc.subjectNeutrophils-
Palavras-chave: dc.subjectTaurine dibromamine-
Título: dc.titleInhibition of lysozyme by taurine dibromamine-
Tipo de arquivo: dc.typelivro digital-
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