Low Molecular Weight, Sequence Based, Collagenase Inhibitors Selectively Block the Interaction Between Collagenase and TIMP (Tissue Inhibitor of Metalloproteinases)
| Autor: | Didier Faucher, Terence Cartwright, Yves Lelièvre, Romaine Bouboutou, Daniel Achard, J. Boiziau |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
MMP1
Matrix metalloproteinase Substrate Specificity Structure-Activity Relationship Stereospecificity Rheumatology medicine Animals Amino Acid Sequence Glycoproteins chemistry.chemical_classification Metalloproteinase Binding Sites biology Metalloendopeptidases Active site Stereoisomerism Tissue Inhibitor of Metalloproteinases Molecular Weight Microbial Collagenase Enzyme chemistry Biochemistry Enzyme inhibitor biology.protein Collagenase Cattle Amino Acids Branched-Chain Protein Binding medicine.drug |
| Zdroj: | Matrix. 10:292-299 |
| ISSN: | 0934-8832 |
| DOI: | 10.1016/s0934-8832(11)80184-8 |
| Popis: | Sequence-based inhibitors of collagenase bearing an hydroxamate group capable of chelating the active site zinc atom were synthesized and tested. The effect of one of these molecules (RP 59 794; Ki about 10- 8 M) on the formation of the TIMP: collagenase complex was also tested. RP 59 794 blocks complex formation and can partially dissociate established TIMP: collagenase complexes. It exhibits the same stereospecificity in this activity as in its inhibition of collagenase suggesting that TIMP and RP 59 794 both interact with the active site region of collagenase. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|