Structure-based design and synthesis of a series of hydroxamic acids with a quaternary-hydroxy group in P1 as inhibitors of matrix metalloproteinases

DOI: 10.1016/S0960-894X(98)00125-5

Source and publish data:

Bioorganic and Medicinal Chemistry Letters p. 837 - 842 (1998)

Update date:2022-08-05

Topics:

Authors:

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.

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Article abstract of DOI:10.1016/S0960-894X(98)00125-5

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.

Full text of DOI:10.1016/S0960-894X(98)00125-5

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