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1: Bioorg Med Chem Lett. 2008 Jun 15;18(12):3646-51. Epub 2008 May 1.
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Design, synthesis, and evaluation of inhibitors of cathepsin L: Exploiting a unique thiocarbazate chemotype.

Myers MC, Shah PP, Beavers MP, Napper AD, Diamond SL, Smith AB 3rd, Huryn DM.

Penn Center for Molecular Discovery, University of Pennsylvania, 1024 Vagelos Research Laboratories, Philadelphia, PA 19104-6383, USA.

Recently, we identified a thiocarbazate that exhibits potent inhibitory activity against human cathepsin L. Since this structure represents a novel chemotype with potential for activity against the entire cysteine protease family, we designed, synthesized, and assayed a series of analogs to probe the mechanism of action, as well as the structural requirements for cathepsin L activity. Molecular docking studies using coordinates of a papain-inhibitor complex as a model for cathepsin L provided useful insights.

Publication Types:
PMID: 18499453 [PubMed - indexed for MEDLINE]

PMCID: PMC2494853 [Available on 06/15/09]