Peptides based on the conserved predomain sequence of matrix metalloproteinases inhibit human stromelysin and collagenase
| Autor: | N. Fotouhi, Robert L. Walsky, A. Lugo, A. C. Hanglow, M. B. Finch-Arietta, L. Lusch, M. Visnick |
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| Rok vydání: | 1993 |
| Předmět: |
Magnetic Resonance Spectroscopy
Immunology Molecular Sequence Data Peptide Matrix metalloproteinase Matrix Metalloproteinase Inhibitors Toxicology Pentapeptide repeat Stromelysin 1 Mass Spectrometry Zymogen medicine Humans Pharmacology (medical) Amino Acid Sequence Cysteine Chromatography High Pressure Liquid Pharmacology chemistry.chemical_classification Enzyme Precursors Tetrapeptide Metalloendopeptidases Molecular biology Peptide Fragments Amino acid chemistry Biochemistry Collagenase Matrix Metalloproteinase 3 medicine.drug |
| Zdroj: | Agents and actions. |
| ISSN: | 0065-4299 |
| Popis: | Prostromelysin, a member of the family of matrix metalloproteinases, is secreted as a zymogen which is activated after cleavage of the His81-Phe82 bond. The 82 amino acid propeptide that is removed during activation contains 12 amino acids, MRKPRC75GVPDVG, that are highly conserved in all MMPs. We evaluated a series of peptides that span this region for their ability to inhibit stromelysin. The hexapeptide, Ac-RCGVPD, and the pentapeptide, Ac-RCGVP had IC50 values of approx. 10 microM. The tetrapeptide, Ac-RCGV, was somewhat less potent with an IC50 of 60 microM. Smaller peptides, e.g. Ac-RCG, were significantly less potent as inhibitors. Substitutions of Cys75 with Ser resulted in a complete loss of inhibitory activity. The peptides in this series also inhibited human fibroblast collagenase. |
| Databáze: | OpenAIRE |
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