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Peptidyl epoxides extended in the P' direction as cysteine protease inhibitors: effect on affinity and mechanism of inhibition.

Perlman, Nurit; Hazan, Maya; Shokhen, Michael; Albeck, Amnon.
Bioorg Med Chem ; 16(19): 9032-9, 2008 Oct 01.
Artículo en Inglés | MEDLINE | ID: mdl-18789705
Endo peptidyl epoxides, in which the central epoxidic moiety replaces the scissile amide bond of a P(3)-P(3)' peptide, were designed as cysteine proteases inhibitors. The additional P'-S' interactions, relative to those of an exo peptidyl epoxide of the same P(3)-P(1) sequence, significantly improved affinity to the enzymes papain and cathepsin B, but also changed the mode of inhibition from active-site directed inactivation to reversible competitive inhibition. Computational models rationalize the binding affinity and the inhibition mechanism.