Literature DB >> 7945258

Phosphinic peptide analogues as potent inhibitors of Corynebacterium rathayii bacterial collagenase.

A Yiotakis1, A Lecoq, A Nicolaou, J Labadie, V Dive.   

Abstract

Pseudo-substrate analogues of collagenase from Corynebacterium rathayii, in which the scissile peptide bond is replaced by a phosphinic moiety, were synthesized and evaluated as inhibitors of this enzyme. The phosphinic tetrapeptide, Z-Phe-psi(PO2CH2)-Gly-Pro-Nle (1), was found to be a potent inhibitor of collagenase with a Ki value of 8 nM. Increasing the length of the phosphinic-containing inhibitors from tetra- to hepta-peptide size further improves the potency of these compounds. The heptapeptide analogue, Z-Phe-Gly-Pro-Phe-psi(PO2CH2)-Gly-Pro-Nle-OMe, with a Ki value of 0.6 nM, is the most potent inhibitor reported to date for bacterial collagenases. A comparison between the phosphinic analogue Z-Phe-psi(PO2CH2)-Gly-Pro-Nle (1) and the phosphonamide peptide Z-Phe-psi(PO2NH)-Gly-Pro-Nle (2) shows that for bacterial collagenase the replacement of a CH2 by an NH group results only in a modest increase in affinity from Ki = 8 nM for compound 1 to Ki = 6 nM for compound 2. Most of the phosphorus-containing inhibitors of this series are slow- or slow-tight-binding inhibitors with second-order rate constants for association and dissociation varying respectively for the kon values from 1 x 10(3) to 26 x 10(3) M-1.s-1 and for the koff values from 3 x 10(-4) to 2 x 10(-5) s-1. Interestingly, the lower affinity of the molecule containing a D residue in the P1 position of the inhibitor, compared with the molecule with an L residue in this position, is mainly the consequence of a lower rate constant for association of these D stereoisomers with the enzyme. This study demonstrates that phosphinic peptide analogues are potent inhibitors of a bacterial collagenase. The development of new phosphinic peptides should lead to the discovery of potent inhibitors of other zinc metalloproteases. Details of how the analogues were synthesized are given in Supplementary Publication SUP 50176 (14 pages), which has been deposited with the British Library Document Supply Centre, Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, from whom copies can be obtained on the terms indicated in Biochem. J. (1994) 297, 9.

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Year:  1994        PMID: 7945258      PMCID: PMC1137593          DOI: 10.1042/bj3030323

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  33 in total

1.  Tight-binding inhibitors-I. Kinetic behavior.

Authors:  S Cha
Journal:  Biochem Pharmacol       Date:  1975-12-01       Impact factor: 5.858

2.  Limited proteolysis of type I collagen at hyperreactive sites by class I and II Clostridium histolyticum collagenases: complementary digestion patterns.

Authors:  M F French; K A Mookhtiar; H E Van Wart
Journal:  Biochemistry       Date:  1987-02-10       Impact factor: 3.162

3.  Complementary substrate specificities of class I and class II collagenases from Clostridium histolyticum.

Authors:  H E Van Wart; D R Steinbrink
Journal:  Biochemistry       Date:  1985-11-05       Impact factor: 3.162

4.  Conditions of production and properties of the collagenolytic enzymes by two Bacillus strains from dental plaque.

Authors:  E Söderling; K U Paunio
Journal:  J Periodontal Res       Date:  1981-09       Impact factor: 4.419

5.  A continuous spectrophotometric assay for Clostridium histolyticum collagenase.

Authors:  H E Van Wart; D R Steinbrink
Journal:  Anal Biochem       Date:  1981-05-15       Impact factor: 3.365

6.  Pathogenesis of serratial infection: activation of the Hageman factor-prekallikrein cascade by serratial protease.

Authors:  K Matsumoto; T Yamamoto; R Kamata; H Maeda
Journal:  J Biochem       Date:  1984-09       Impact factor: 3.387

7.  Evaluation of methods for estimating the dissociation constant of tight binding enzyme inhibitors.

Authors:  W R Greco; M T Hakala
Journal:  J Biol Chem       Date:  1979-12-10       Impact factor: 5.157

8.  New thiol inhibitor of Achromobacter iophagus collagenase. Specificity of the enzyme's S3' subsite.

Authors:  A Yiotakis; V Dive
Journal:  Eur J Biochem       Date:  1986-10-15

9.  Phosphonamidates as transition-state analogue inhibitors of thermolysin.

Authors:  P A Bartlett; C K Marlowe
Journal:  Biochemistry       Date:  1983-09-27       Impact factor: 3.162

10.  Binding energetics of phosphorus-containing inhibitors of thermolysin.

Authors:  D Grobelny; U B Goli; R E Galardy
Journal:  Biochemistry       Date:  1989-06-13       Impact factor: 3.162

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  3 in total

1.  RXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites.

Authors:  V Dive; J Cotton; A Yiotakis; A Michaud; S Vassiliou; J Jiracek; G Vazeux; M T Chauvet; P Cuniasse; P Corvol
Journal:  Proc Natl Acad Sci U S A       Date:  1999-04-13       Impact factor: 11.205

2.  Phosphinic peptides, the first potent inhibitors of astacin, behave as extremely slow-binding inhibitors.

Authors:  I Yiallouros; S Vassiliou; A Yiotakis; R Zwilling; W Stöcker; V Dive
Journal:  Biochem J       Date:  1998-04-15       Impact factor: 3.857

3.  Phosphorus-containing peptides as mixed inhibitors of endopeptidase 3.4.24.15 and 3.4.24.16: effect on neurotensin degradation in vitro and in vivo.

Authors:  B Vincent; V Dive; A Yiotakis; C Smadja; R Maldonado; J P Vincent; F Checler
Journal:  Br J Pharmacol       Date:  1995-07       Impact factor: 8.739

  3 in total

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