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

Swati S. More; Robert Vince

doi:10.1016/j.bmcl.2006.12.056

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

Swati S. More, Robert Vince

Center for Drug Design

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18 Scopus citations

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 β-keto ester compounds are reported.

Original language	English (US)
Pages (from-to)	3793-3797
Number of pages	5
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	17
Issue number	13
DOIs	https://doi.org/10.1016/j.bmcl.2006.12.056
State	Published - Jul 1 2007

Bibliographical note

Funding Information:
This work was supported by the funding from the Center for Drug Design, Academic Health Center, University of Minnesota.

Keywords

Ethyl acetoacetate
Glutathione
Glyoxalase
Methylglyoxal
Transition-state inhibitor
β-Keto ester

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KW - Methylglyoxal

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KW - β-Keto ester

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

Abstract

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Keywords

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