Hydroxamate derivatives of substrate-analogous peptides containing aminomalonic acid are potent inhibitors of matrix metalloproteinases

Krumme D, Wenzel H, Tschesche H (1998)
FEBS LETTERS 436(2): 209-212.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Abstract / Bemerkung
Novel peptides containing the sequence -Pro-Leu-Ama(NHOH)- were synthesized and characterized by spectroscopic techniques. Their inhibitory properties towards the activated form of native human gelatinase B (MMP-9) and the catalytic domain of neutrophil collagenase (cdMMP-8) were determined. The most effective inhibitor synthesized exhibits K-i values of 2 x 10(-6) Il I (cdMMP-8) and 5 x 10(-9) RI (MMP-9) thus attaining interesting discrimination between the tested metalloproteinases. A most important feature of this type of inhibitor is its peptide nature making the compounds similar to natural substrates. In spite of the peptide character of the inhibitors synthesized, the P-1-P-1'-peptide bond shows a high resistance to cleavage by the proteinases. (C) 1998 Federation of European Biochemical Societies.
Stichworte
aminomalonic acid; peptide inhibitor; matrix metalloproteinase; inhibition; hydroxamate
Erscheinungsjahr
1998
Zeitschriftentitel
FEBS LETTERS
Band
436
Ausgabe
2
Seite(n)
209-212
ISSN
0014-5793
Page URI
https://pub.uni-bielefeld.de/record/1624672

Zitieren

Krumme D, Wenzel H, Tschesche H. Hydroxamate derivatives of substrate-analogous peptides containing aminomalonic acid are potent inhibitors of matrix metalloproteinases. FEBS LETTERS. 1998;436(2):209-212.
Krumme, D., Wenzel, H., & Tschesche, H. (1998). Hydroxamate derivatives of substrate-analogous peptides containing aminomalonic acid are potent inhibitors of matrix metalloproteinases. FEBS LETTERS, 436(2), 209-212. https://doi.org/10.1016/S0014-5793(98)01128-4
Krumme, D, Wenzel, Herbert, and Tschesche, Harald. 1998. “Hydroxamate derivatives of substrate-analogous peptides containing aminomalonic acid are potent inhibitors of matrix metalloproteinases”. FEBS LETTERS 436 (2): 209-212.
Krumme, D., Wenzel, H., and Tschesche, H. (1998). Hydroxamate derivatives of substrate-analogous peptides containing aminomalonic acid are potent inhibitors of matrix metalloproteinases. FEBS LETTERS 436, 209-212.
Krumme, D., Wenzel, H., & Tschesche, H., 1998. Hydroxamate derivatives of substrate-analogous peptides containing aminomalonic acid are potent inhibitors of matrix metalloproteinases. FEBS LETTERS, 436(2), p 209-212.
D. Krumme, H. Wenzel, and H. Tschesche, “Hydroxamate derivatives of substrate-analogous peptides containing aminomalonic acid are potent inhibitors of matrix metalloproteinases”, FEBS LETTERS, vol. 436, 1998, pp. 209-212.
Krumme, D., Wenzel, H., Tschesche, H.: Hydroxamate derivatives of substrate-analogous peptides containing aminomalonic acid are potent inhibitors of matrix metalloproteinases. FEBS LETTERS. 436, 209-212 (1998).
Krumme, D, Wenzel, Herbert, and Tschesche, Harald. “Hydroxamate derivatives of substrate-analogous peptides containing aminomalonic acid are potent inhibitors of matrix metalloproteinases”. FEBS LETTERS 436.2 (1998): 209-212.

11 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

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PMID: 22143909
Rational design of tropoelastin peptide-based inhibitors of metalloproteinases.
Jensen SA, Andersen P, Vrhovski B, Weiss AS., Arch Biochem Biophys 409(2), 2003
PMID: 12504900
General synthesis of alpha-substituted 3-bisaryloxy propionic acid derivatives as specific MMP inhibitors.
Chollet AM, Le Diguarher T, Murray L, Bertrand M, Tucker GC, Sabatini M, Pierré A, Atassi G, Bonnet J, Casara P., Bioorg Med Chem Lett 11(3), 2001
PMID: 11212095
Determination of matrix metalloproteinase activity using biotinylated gelatin.
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PMID: 11038285

16 References

Daten bereitgestellt von Europe PubMed Central.

Matrix metalloproteinases: a review.
Birkedal-Hansen H, Moore WG, Bodden MK, Windsor LJ, Birkedal-Hansen B, DeCarlo A, Engler JA., Crit. Rev. Oral Biol. Med. 4(2), 1993
PMID: 8435466
Collagenase inhibitors: their design and potential therapeutic use.
Johnson WH, Roberts NA, Borkakoti N., J. Enzym. Inhib. 2(1), 1987
PMID: 2854154
Synthetic inhibitors of bacterial and mammalian interstitial collagenases.
Schwartz MA, Van Wart HE., Prog Med Chem 29(), 1992
PMID: 1475372
Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor.
Grams F, Crimmin M, Hinnes L, Huxley P, Pieper M, Tschesche H, Bode W., Biochemistry 34(43), 1995
PMID: 7577999
Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor.
Borkakoti N, Winkler FK, Williams DH, D'Arcy A, Broadhurst MJ, Brown PA, Johnson WH, Murray EJ., Nat. Struct. Biol. 1(2), 1994
PMID: 7656013
1.56 A structure of mature truncated human fibroblast collagenase.
Spurlino JC, Smallwood AM, Carlton DD, Banks TM, Vavra KJ, Johnson JS, Cook ER, Falvo J, Wahl RC, Pulvino TA., Proteins 19(2), 1994
PMID: 8090713
On the size of the active site in proteases. I. Papain.
Schechter I, Berger A., Biochem. Biophys. Res. Commun. 27(2), 1967
PMID: 6035483

AUTHOR UNKNOWN, 0
Latent collagenase and gelatinase from human neutrophils and their activation.
Tschesche H, Knauper V, Kramer S, Michaelis J, Oberhoff R, Reinke H., Matrix Suppl 1(), 1992
PMID: 1480034
The recombinant catalytic domain of human neutrophil collagenase lacks type I collagen substrate specificity.
Schnierer S, Kleine T, Gote T, Hillemann A, Knauper V, Tschesche H., Biochem. Biophys. Res. Commun. 191(2), 1993
PMID: 8460992
The determination of enzyme inhibitor constants.
DIXON M., Biochem. J. 55(1), 1953
PMID: 13093635
Synthetic substrates of vertebrate collagenase.
Weingarten H, Martin R, Feder J., Biochemistry 24(23), 1985
PMID: 3002449

Fields, J. Biol. Chem. 262(), 1973
Sequence specificities of human fibroblast and neutrophil collagenases.
Netzel-Arnett S, Fields GB, Birkedal-Hansen H, Van Wart HE, Fields G., J. Biol. Chem. 266(11), 1991
PMID: 1849891
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