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ID: ALA1139302
Journal: Bioorg Med Chem Lett
Title: Modification of the N-terminal sulfonyl residue in 3-amidinophenylalanine-based matriptase inhibitors.
Authors: Steinmetzer T, Dönnecke D, Korsonewski M, Neuwirth C, Steinmetzer P, Schulze A, Saupe SM, Schweinitz A.
Abstract: Replacement of the N-terminal beta-alanyl-amide moiety in previously identified matriptase inhibitors by non-charged aryl groups caused a slightly decreased potency and partially reduced selectivity, especially towards thrombin. However, some of these analogues are still potent matriptase inhibitors with K(i)-values <10nM. In contrast, improved activity was observed for newly designed tribasic analogues, especially for compound 21, which inhibits matriptase with an K(i)-value of 80pM.
CiteXplore: 19036586