The specificity of the immune response relies on processing of foreign proteins and presentation of antigenic peptides at the cell surface. Inhibition of antigen presentation, and the subsequent activation of T-cells, should, in theory, modulate the immune response. The cysteine protease Cathepsin S performs a fundamental step in antigen presentation and therefore represents an attractive target for inhibition. Herein, we report a series of potent and reversible Cathepsin S inhibitors based on dipeptide nitriles. These inhibitors show nanomolar inhibition of the target enzyme as well as cellular potency in a human B cell line. The first X-ray crystal structure of a reversible inhibitor cocrystallized with Cathepsin S is also reported.
From the corresponding TpMo(CO) 2 (π-allyl) complexes, four symmetrically substituted TpMo(CO)(NO)(π-allyl) + complexes (π-allyl ) propenyl, 2-methylpropenyl, cyclohexenyl, and cyclooctenyl) were prepared and characterized by IR, by 1 H and 13 C NMR spectroscopy, and in one case by X-ray crystallography. The BF 4 -salts of the cationic nitrosyl complexes were unstable in solution; however, using the noncoordinating counterion [(3,5-(CF 3 ) 2 C 6 H 3 ) 4 B] -
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