Author |
Matsuo, Alisson L.
![]() Carmona, Adriana K. ![]() Silva, Luiz S. ![]() Cunha, Carlos E. L. ![]() Nakayasu, Ernesto S. ![]() Almeida, Igor C. ![]() Juliano, Maria A. ![]() Puccia, Rosana ![]() |
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 Npys |
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 |
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Access rights | Closed access |
Type | Article |
Web of Science ID | WOS:000245115000025 |
URI | http://repositorio.unifesp.br/handle/11600/29670 |
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