Sang Yankui, Shi Qing, Mo Mingguang, Ni Caixia, Li Zonghe, Liu Bichong, Deng Qishan, Creighton Donald J, Zheng Zhe-Bin
Department of Antibiotic Research & Re-evaluation, Key Laboratory of Sichuan Province, Sichuan Industrial Institute of Antibiotics, Chengdu University, Huaguan Road 168, Chengdu City, Sichuan Province 610052, PR China.
Department of Chemistry & Biochemistry, University of Maryland Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21250, USA.
Bioorg Med Chem Lett. 2015 Nov 1;25(21):4724-4727. doi: 10.1016/j.bmcl.2015.08.055. Epub 2015 Aug 20.
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.
锌金属酶乙二醛酶I（GlxI）催化细胞毒性甲基乙二醛的谷胱甘肽依赖性失活。基于过渡态类似物S-（N-溴苯基-N-羟基氨基甲酰基）谷胱甘肽（BHG）合成了两种竞争性二价GlxI抑制剂，聚BHG2-62（Ki = 1.0 nM）和聚BHG2-54（Ki = 0.3 nM）。最有效的抑制剂聚BHG2-54是GlxI的首个亚纳摩尔抑制剂，其效力比BHG本身强50倍以上。
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