257933-90-7Relevant academic research and scientific papers
N-aryl sulfonyl homocysteine hydroxamate inhibitors of matrix metalloproteinases: Further probing of the S1, S1′, and S2′ pockets
Hanessian,Moitessier,Gauchet,Viau
, p. 3066 - 3073 (2007/10/03)
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.
Picking the S1, S1' and S2' pockets of matrix metalloproteinases. A niche for potent acyclic sulfonamide inhibitors.
Hanessian,Bouzbouz,Boudon,Tucker,Peyroulan
, p. 1691 - 1696 (2007/10/03)
A series of acyclic hydroxamic acids harboring strategically placed alpha-arylsulfonamido and thioether groups was synthesized and found to be potent inhibitors of various MMPs. An unprecedented cleavage of t-butyl hydroxamates to hydroxamic acids was found.
