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ID: ALA1136973

Journal: Bioorg Med Chem Lett

Title: Structure-activity relationships of heteroaromatic esters as human rhinovirus 3C protease inhibitors.

Authors: Im I, Lee ES, Choi SJ, Lee JY, Kim YC.

Abstract: Human rhinovirus 3C protease (HRV 3C(pro)) is known to be a promising target for development of therapeutic agents against the common cold because of the importance of the protease in viral replication as well as its expression in a large number of serotypes. To explore non-peptidic inhibitors of HRV 3C(pro), a series of novel heteroaromatic esters was synthesized and evaluated for inhibitory activity against HRV 3C(pro), to determine the structure-activity relationships. The most potent inhibitor, 7, with a 5-bromopyridinyl group, had an IC(50) value of 80nM. In addition, the binding mode of a novel analog, 19, with the 4-hydroxyquinolinone moiety, was explored by molecular docking, suggesting a new interaction in the S1 pocket.

CiteXplore: 19464175

DOI: 10.1016/j.bmcl.2009.04.114