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

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

Author Matsuo, Alisson L. Google Scholar
Carmona, Adriana K. Google Scholar
Silva, Luiz S. Google Scholar
Cunha, Carlos E. L. Google Scholar
Nakayasu, Ernesto S. Google Scholar
Almeida, Igor C. Google Scholar
Juliano, Maria A. Google Scholar
Puccia, Rosana Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Univ Texas
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.
Keywords Paracoccidiodes brasiliensis
serine-thiol proteinase
Language English
Date 2007-04-20
Published in Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 355, n. 4, p. 1000-1005, 2007.
ISSN 0006-291X (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 1000-1005
Origin http://dx.doi.org/10.1016/j.bbrc.2007.02.070
Access rights Closed access
Type Article
Web of Science ID WOS:000245115000025
URI http://repositorio.unifesp.br/handle/11600/29670

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