2. Academic Validation
  3. Design, synthesis, and binding studies of bidentate Zn-chelating peptidic inhibitors of glyoxalase-I

Design, synthesis, and binding studies of bidentate Zn-chelating peptidic inhibitors of glyoxalase-I

  • Bioorg Med Chem Lett. 2007 Jul 1;17(13):3793-7. doi: 10.1016/j.bmcl.2006.12.056.
Swati S More 1,  Robert Vince
Affiliations

Affiliation

  • 1 Center for Drug Design, Academic Health Center, and Department of Medicinal Chemistry, College of Pharmacy, University of Minnesota, Minneapolis, MN 55455, USA.
PMID: 17513107 DOI: 10.1016/j.bmcl.2006.12.056
Abstract

The known affinity of ethyl acetoacetate (ACC) toward divalent zinc prompted us to attempt its employment as a chelating moiety in the design of glyoxalase-I inhibitors. A practical synthetic route was developed to incorporate this pharmacophore into the side chain of glutamic acid, with flexibility to allow incorporation of additional functionality at the end-stage of the synthesis. Herein, the details of this synthetic approach as well as the evaluation of the resultant beta-keto ester compounds are reported.

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