2. Academic Validation
  3. Exploration of cathepsin S inhibitors characterized by a triazole P1-P2 amide replacement

Exploration of cathepsin S inhibitors characterized by a triazole P1-P2 amide replacement

  • Bioorg Med Chem Lett. 2012 Dec 1;22(23):7189-93. doi: 10.1016/j.bmcl.2012.09.054.
Neil Moss 1,  Zhaoming Xiong,  Mike Burke,  Derek Cogan,  Donghong A Gao,  Kathleen Haverty,  Alexander Heim-Riether,  Eugene R Hickey,  Raj Nagaraja,  Matthew Netherton,  Kathy O'Shea,  Philip Ramsden,  Racheline Schwartz,  Daw-Tsun Shih,  Yancey Ward,  Erick Young,  Qing Zhang
Affiliations

Affiliation

  • 1 Department of Medicinal Chemistry, Immunology and Inflammation, Boehringer Ingelheim Pharmaceutical, Inc., 900 Ridgebury Road, Ridgefield, CT 06877, USA. Neil.Moss@comcast.com
PMID: 23084902 DOI: 10.1016/j.bmcl.2012.09.054
Abstract

This paper details exploration of a class of triazole-based Cathepsin S inhibitors originally reported by Ellman and co-workers. SAR studies involving modifications across the whole inhibitor provide a perspective on the strengths and weaknesses of this class of inhibitors. In addition, we put the unique characteristics of this class of compounds into perspective with Other classes of Cathepsin S inhibitors.

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