A covalent G-site inhibitor for glutathione S-transferase Pi (GSTP 1-1 )

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 formati...

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Veröffentlicht in:	Chemical communications (Cambridge, England) England), 2017-10, Vol.53 (81), p.11138-11141
Hauptverfasser:	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
Format:	Artikel
Sprache:	eng
Schlagworte:	Dose-Response Relationship, Drug Enzyme Inhibitors - chemical synthesis Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology Glutathione S-Transferase pi - antagonists & inhibitors Glutathione S-Transferase pi - metabolism Humans Molecular Dynamics Simulation Molecular Structure Structure-Activity Relationship
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Zusammenfassung:	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.
ISSN:	1359-7345 1364-548X
DOI:	10.1039/c7cc05829b