Chem. J. Chinese Universities ›› 2012, Vol. 33 ›› Issue (05): 983.doi: 10.3969/j.issn.0251-0790.2012.05.021

• Biological Chemistry • Previous Articles     Next Articles

A Tetrapeptide Containing Selenium(SecRGD) with Glutathione Peroxidase Activity

ZOU Xian-Feng1,2, LV Shao-Wu1   

  1. 1. Key Laboratory for Molecular Enzymology and Engineering, Ministry of Education, Jilin University, Changchun 130012, China;
    2. Key Laboratory for Agricultural Products Processing of Jilin Province Ordinary University, Changchun University, Changchun 130022, China
  • Received:2011-06-24 Online:2012-05-10 Published:2012-05-10

Abstract: Glutathione peroxidase(GPx) is the most crucial antioxidant enzyme in a variety of organisms. Here, base on the Arg-Gly-Asp(RGD), a tetrapeptide containing selenium(SeCRGD) was chemically synthesized. The existential state of the peptide was investigated by ESI-MS and hydride generation atom fluorescence spectral analysis. The GPx activities and the kinetics of the peptide were determined by the enzyme coupling method. The antioxidant effect of the peptide was evaluated based on MTT assay. The results showed that a kind of oxide form, SecRGD-dimer, was confirmed by ESI-MS and selenium content analysis. The peptide had GPx activity of 5.54 U/μmol and more than that of Ebselen. As native enzyme, a ping-pong mechanism was observed in steady-state kinetics studies. Moreover, the novel selenopeptide occupied merits of small molecular weight, good solubility in water and low toxicity. Especially, the peptide was found that could protect Vero cells from the injury induced by H2O2. Thus, the novel selenopeptide possesses a good potential in medicinal application.

Key words: Glutathione peroxidase, Selenopeptide, Antioxidant activity

CLC Number: 

TrendMD: