| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10593604 | Bioorganic & Medicinal Chemistry Letters | 2015 | 6 Pages |
Abstract
The zinc metalloenzyme glyoxalase I (GlxI) catalyzes the glutathione-dependent inactivation of cytotoxic methylglyoxal. Two competitive bivalent GlxI inhibitors, polyBHG2-62 (Ki = 1.0 nM) and polyBHG2-54 (Ki = 0.3 nM), were synthesized based on the transition-state analog S-(N-bromophenyl-N-hydroxycarbamoyl) glutathione (BHG). The most effective inhibitor, polyBHG2-54, is the first subnanomolar inhibitor of GlxI, and is over 50-fold more potent than BHG itself.90
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Authors
Yankui Sang, Qing Shi, Mingguang Mo, Caixia Ni, Zonghe Li, Bichong Liu, Qishan Deng, Donald J. Creighton, Zhe-Bin Zheng,