Inhibition of Human Stromelysin by Peptides Based on the N-Terminal Domain of Tissue Inhibitor of Metalloproteinases-1
| Autor: | A. Lugo, Robert L. Walsky, M. Visnick, N. Fotouhi, A. C. Hanglow, John W. Coffey |
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| Rok vydání: | 1994 |
| Předmět: |
Matrix Metalloproteinase 3
Matrix metalloproteinase inhibitor Molecular Sequence Data Biophysics Matrix Metalloproteinase Inhibitors Matrix metalloproteinase Peptides Cyclic Biochemistry Protein Structure Secondary Epitope Structure-Activity Relationship Protein structure Humans Structure–activity relationship Amino Acid Sequence Molecular Biology Peptide sequence Glycoproteins Chemistry Metalloendopeptidases Tissue Inhibitor of Metalloproteinases Cell Biology Molecular biology Indicators and Reagents Peptides Oligopeptides Cysteine |
| Zdroj: | Biochemical and Biophysical Research Communications. 205:1156-1163 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1994.2787 |
| Popis: | The tissue inhibitors of metalloproteinases (TIMPs) represent a family of naturally occurring protein inhibitors of stromelysin and other members of the family of matrix metalloproteinases. A series of peptides based on the N-terminal sequence of natural TIMP-1 was synthesized and assessed for inhibitory activity against purified human stromelysin. Inhibitor peptides were identified in the loop (bounded by the disulfide bonds [C3-C99] and [C13-C124]), e.g., [C3(Acm)-C13], (IC50, 42 microM). It was established that inhibition was due to the free sulfhydryl group of either C13 or C124. However, peptides within [C70(Acm)-C98(Acm)] inhibited stromelysin independently of zinc co-ordination by cysteine. The binding epitope in TIMP-1 may be discontinuous and comprised of sequences from at least 2 loops. |
| Databáze: | OpenAIRE |
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