Low molecular weight, sequence based, collagenase inhibitors selectively block the interaction between collagenase and TIMP (tissue inhibitor of metalloproteinases).

Y Lelièvre; R Bouboutou; J Boiziau; D Faucher; D Achard; T Cartwright

doi:10.1016/s0934-8832(11)80184-8

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Low molecular weight, sequence based, collagenase inhibitors selectively block the interaction between collagenase and TIMP (tissue inhibitor of metalloproteinases).

Y Lelièvre·R Bouboutou·J Boiziau·D Faucher·D Achard·T Cartwright

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Abstract

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 59794; Ki about 10(-8) M) on the formation of the TIMP: collagenase complex was also tested. RP 59794 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 59794 both interact with the active site region of collagenase.

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Amino Acid Sequence Amino Acids, Branched-Chain Animals Binding Sites Cattle Glycoproteins Metalloendopeptidases Microbial Collagenase Molecular Weight Protein Binding Stereoisomerism Structure-Activity Relationship Substrate Specificity Tissue Inhibitor of Metalloproteinases Comparative Study Journal Article

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Y Lelièvre, R Bouboutou, J Boiziau, D Faucher, D Achard, T Cartwright. 1990. Low molecular weight, sequence based, collagenase inhibitors selectively block the interaction between collagenase and TIMP (tissue inhibitor of metalloproteinases).. https://doi.org/10.1016/s0934-8832(11)80184-8

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