Antioxidant functions of selenoenzyme glutathione peroxidase (GPx) can be imitated by using a wide range of small organic selenium compounds. However, the GPx-like antioxidant activities of selenocysteine (Sec) derivatives as well as Sec-containing peptides have rarely been investigated in literature, despite the expectation that they would serve as useful probes or models for understanding the molecular mechanisms of the GPx antioxidant functions. In our laboratory, we focus on the synthesis of various selenoamino acid derivatives and their applications to selenopeptide synthesis as well as on the evaluation as GPx models.Selenoglutathione (GSeH) was obtained as an oxidized diselenide form by solid-phase peptide synthesis. Comparison of the GPx activity against hydrogen peroxide with that of other selenopeptides revealed unusually high antioxidant activity of GSeH. The unique redox properties were rationalized by characterization of the redox cycle involving the activated intermediates.

Modeling antixidant function of glutathione peroxidase by using selenopeptides

244th National Meeting (2012)

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