Shishido Yuko, Tomoike Fumiaki, Kimura Yasuaki, Kuwata Keiko, Yano Takato, Fukui Kenji, Fujikawa Haruka, Sekido Yoshitaka, Murakami-Tonami Yuko, Kameda Tomoshi, Shuto Satoshi, Abe Hiroshi
Department of Chemistry, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-Ku, Nagoya, 464-8602, Japan.
Chem Commun (Camb). 2017 Oct 10;53(81):11138-11141. doi: 10.1039/c7cc05829b.
We herein report the first covalent G-site-binding inhibitor for GST, GS-ESF (1), which irreversibly inhibited the GSTP function. LC-MS/MS and X-ray structure analyses of the covalently linked GST-inhibitor complex suggested that 1 reacted with Tyr108 of GSTP. The mechanism of covalent bond formation was discussed based on MD simulation results.
我们在此报告首个针对谷胱甘肽S-转移酶（GST）的共价G位点结合抑制剂GS-ESF（1），它不可逆地抑制了GSTP的功能。对共价连接的GST-抑制剂复合物进行的液相色谱-串联质谱（LC-MS/MS）和X射线结构分析表明，1与GSTP的Tyr108发生了反应。基于分子动力学（MD）模拟结果讨论了共价键形成的机制。
