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Gene manipulation based selenium-containing peptide exhibiting synergism of SOD and GPx

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Chemical Research in Chinese Universities Aims and scope

Abstract

In this paper, we constructed a novel bifunctional superoxide dismutase(SOD)/glutathione peroxidase(GPx) mimic, a selenium-, copper-containing 35-mer peptide conjugate(Se-Cu-35P) in which a three-amino acid linker(Gly-Asn-Gly) connects the C-terminus of 17-mer polypeptide SOD mimic with the N-terminus of 15-mer polypeptide GPx mimic. The SOD and GPx activities of Se-Cu-35P are two orders of magnitude lower than those of natural SOD and GPx, respectively. It provides a GPx activity 56-fold higher than Ebselen(a well-known GPx mimic). The glutathione(GSH) binding constant is 5.6×102 L·mol−1. Se-Cu-35P synergistically resists against the inactivation by H2O2 and protects the mitochondria from oxidative damage in a dose dependent manner. These results highlight the challenge of generating an efficient SOD/GPx synergism mimic. It could facilitate the studies of the cooperation of GPx and SOD and could be a potential therapeutic agent for the treatment of ROS-mediated diseases.

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Correspondence to Ganglin Yan or Ying Mu.

Additional information

Supported by the National Natural Science Foundation of China(Nos.31170740, 31270907) and the Natural Science Foundation of Jilin Province, China(No.20130101159JC).

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Shen, N., Yan, F., Lü, S. et al. Gene manipulation based selenium-containing peptide exhibiting synergism of SOD and GPx. Chem. Res. Chin. Univ. 30, 947–952 (2014). https://doi.org/10.1007/s40242-014-4239-z

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  • DOI: https://doi.org/10.1007/s40242-014-4239-z

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