Imprinted Human Serum Albumin with Antioxidant Activity

In order to create a new mimic of glutathione peroxidase(GPx), bioimprinting was used to generate gluta-thione(GSH) binding site and chemical modification was used to incorporate catalytic group selenocystine(Sec). Human serum albumin(HSA) and S-substituted dinitrophenyl glutathione(GSH-S-DNP) were...

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Veröffentlicht in:Chemical research in Chinese universities 2011-03, Vol.27 (2), p.258-263
1. Verfasser: SHEN Na YAN Fei GUO Yi LU Shao-wu GONG Ping-sheng XU Ya-wei YAN Gang-lin MU Ying LUO Gui-min
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Sprache:eng
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Zusammenfassung:In order to create a new mimic of glutathione peroxidase(GPx), bioimprinting was used to generate gluta-thione(GSH) binding site and chemical modification was used to incorporate catalytic group selenocystine(Sec). Human serum albumin(HSA) and S-substituted dinitrophenyl glutathione(GSH-S-DNP) were chosen as the imprinted matrix and imprinting template, respectively, to generate a GSH-imprinted protein(GSH-HSA) by bioimprinting. Sec was incorporated into the GSH-HSA by chemical modification to give a new GPx mimic(Se-GSH-HSA). Se-GSH-HSA displayed considerably higher GPx activity than non-printed HSA(Se-HSA). The enzymic properties and kinetics of Se-GSH-HSA were studied. Moreover, Se-GSH-HSA was confirmed to have stronger antioxidant ability to protect mitochondria against oxidative damage with ferrous sulfate/ascorbate-induced mitochondria damage model, indicating that Se-GSH-HSA has potential application in medicine.
ISSN:1005-9040
2210-3171