C-Npys (S-3-nitro-2-pyridinesulfenyl) and peptide derivatives can inhibit a serine-thiol proteinase activity from Paracoccidioides brasiliensis

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dc.contributor.author Matsuo, Alisson L.
dc.contributor.author Carmona, Adriana K.
dc.contributor.author Silva, Luiz S.
dc.contributor.author Cunha, Carlos E. L.
dc.contributor.author Nakayasu, Ernesto S.
dc.contributor.author Almeida, Igor C.
dc.contributor.author Juliano, Maria A.
dc.contributor.author Puccia, Rosana
dc.date.accessioned 2016-01-24T13:48:36Z
dc.date.available 2016-01-24T13:48:36Z
dc.date.issued 2007-04-20
dc.identifier http://dx.doi.org/10.1016/j.bbrc.2007.02.070
dc.identifier.citation Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 355, n. 4, p. 1000-1005, 2007.
dc.identifier.issn 0006-291X
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/29670
dc.description.abstract The inhibitory capacity of C-Npys (S-[3-nitro-2-pyridinesulenyl]) derivatives over thiol-containing serine proteases has never been tested. in the present work we used an extracellular serine-thiol protemase activity from the fungal pathogen Paracoccidio ides brasiliensis (PbST) to describe a potent inhibitory capacity of Bzl-C(Npys)KRLTL-NH2, and Bzl-MKRLTLC(Npys)-NH2. the assays were performed with PbST enriched upon affinity chromatography in a p-aminobenzamidine (pABA)-Sepharose column. Although PbST can cleave the fluorescence resonance energy transfer peptide Abz-MKRLTL-EDDnp between L-T, the C(Npys) derivatives were not substrates nor were they toxic in a cell detachment assay, allowing therapeutic use. the best inhibitor was Bzl-C(Npys)KRLTL-NH2 (K-i = 16 nM), suggesting that the peptide sequence promoted a favorable interaction, especially when C(Npys) was placed at a further position from the L-T bond, at the N-terminus. Inhibition was completely reverted with dithioerythritol, indicating that it was due to the reactivity of the C(Npys) moiety with a free SH- group. (c) 2007 Elsevier Inc. All rights reserved. en
dc.format.extent 1000-1005
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof Biochemical and Biophysical Research Communications
dc.rights Acesso restrito
dc.subject Paracoccidiodes brasiliensis en
dc.subject serine-thiol proteinase en
dc.subject Npys en
dc.title C-Npys (S-3-nitro-2-pyridinesulfenyl) and peptide derivatives can inhibit a serine-thiol proteinase activity from Paracoccidioides brasiliensis en
dc.type Artigo
dc.rights.license http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.contributor.institution Univ Texas
dc.description.affiliation Universidade Federal de São Paulo, Disciplina Biol Celular, Dept Microbiol Immunol & Parasaitol, Cell Biol Div, BR-04023062 São Paulo, Brazil
dc.description.affiliation Universidade Federal de São Paulo, Dept Biophys, BR-04044062 São Paulo, Brazil
dc.description.affiliation Univ Texas, Dept Biol Sci, El Paso, TX 79968 USA
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Disciplina Biol Celular, Dept Microbiol Immunol & Parasaitol, Cell Biol Div, BR-04023062 São Paulo, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Dept Biophys, BR-04044062 São Paulo, Brazil
dc.identifier.doi 10.1016/j.bbrc.2007.02.070
dc.description.source Web of Science
dc.identifier.wos WOS:000245115000025



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