Rapid synthesis of novel dipeptide inhibitors of human collagenase and gelatinase using solid phase chemistry

Abstract Solid phase chemistry expedited the systematic modification of the C and N-terminal groups of cysteine derived lead compound 1 (collagenase IC 50 63nM), providing a series of matrix metalloproteinase inhibitors. Potent inhibitors of collagenase ( 1–2 , 4–6 , and 10–13 ) and gelatinase ( 4–8 ) were identified. Insights into the binding mode of selective inhibitors will be discussed.