Bioorganic and Medicinal Chemistry Letters p. 837 - 842 (1998)
Update date:2022-08-05
Topics:
Jacobson, Irina C.
Reddy, Prabhakar G.
Wasserman, Zelda R.
Hardman, Karl D.
Covington, Maryanne B.
Arner, Elizabeth C.
Copeland, Robert A.
Decicco, Carl P.
Magolda, Ronald L.
Examination of the S1 area of the active site of pro-stromelysin has led us to the design of novel and potent inhibitors of matrix metalloproteinases containing constrained quaternary-hydroxy group at P1. The synthesis and biological activity of these compounds with variations at P1', P2', and P3' will be described.
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