N-aryl sulfonyl homocysteine hydroxamate inhibitors of matrix metalloproteinases: Further probing of the S1, S1′, and S2′ pockets

Article abstract of DOI:10.1021/jm010097f

A series of N-arylsulfonyl S-alkyl homocysteine hydroxamic acids were synthesized with variations in three subsites corresponding to P₁, P₁′, and P₂′. Enzyme assays with a variety of MMPs revealed activity at the low nanomolar level.