153642-83-2Relevant academic research and scientific papers
Inhibition of MMP-1 and MMP-13 with phosphinic acids that exploit binding in the S2 pocket
Reiter, Lawrence A.,Rizzi, James P.,Pandit, Jayvardan,Lasut, Michael J.,McGahee, Shunda M.,Parikh, Vinod D.,Blake, James F.,Danley, Dennis E.,Laird, Ellen R.,Lopez-Anaya, Arturo,Lopresti-Morrow, Lori L.,Mansour, Mahmoud N.,Martinelli, Gary J.,Mitchell, Peter G.,Owens, Brian S.,Pauly, Thomas A.,Reeves, Lisa M.,Schulte, Gayle K.,Yocum, Sue A.
, p. 127 - 132 (1999)
Through the use of empirical and computational methods, phosphinate- based inhibitors of MMP-1 and MMP-13 that bind into the S2 pocket of these enzymes were designed. The synthesis and testing of 2 suggested that binding was occuring as hypothesized. Structure determination of a co-crystal of 2 bound to the catalytic domain of MMP-1 confirmed the binding mode. Substituents binding into S2, S1', S2' and S3', were optimized yielding compounds with low double-digit nM IC50's against these enzymes.
SUBSTITUTED PHOSPHINIC ACID CONTAINING PEPTIDYL DERIVATIVES AS ANTIDEGENERATIVE AGENTS
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, (2008/06/13)
Novel phosphinic acid-containing peptidyl compounds of formula I are found to be useful inhibitors of matrix metalloendoproteinase-mediated diseases including osteoarthritis, rheumatoid arthritis, septic arthritis, tumor invasion in certain cancers, perio
