Abstract
The new GSH analogues H–Glo(–Ser–Gly–OH)–OH ( 5), its O-benzyl derivative 4, and H–Glo(–Asp–Gly–OH)–OH ( 9), characterized by the replacement of central cysteine with either serine or aspartic acid, and containing an urethanic fragment as isosteric substitution of the scissile γ-glutamylic junction, have been synthesized and characterized. Their ability to inhibit human GST P1-1 (hGST P1-1) in comparison with H–Glu(–Ser–Gly–OH)–OH and H–Glu(–Asp–Gly–OH)–OH, which are potent competitive inhibitors of rat GST 3-3 and 4-4, has been evaluated. In order to further investigate the effect of the isosteric substitution on the binding abilities of the new GSH analogues 4, 5 and 9, the previously reported cysteinyl-containing analogue H–Glo(–Cys–Gly–OH)–OH has been also evaluated as a co-substrate for hGSTP1-1.
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