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KMID : 0043320080310111471
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Archives of Pharmacal Research
2008 Volume.31 No. 11 p.1471 ~ p.1476
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Expression of Thymosin α1-thymopentin Fusion Peptide in Pichia pastoris and its Characterization
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Wang Feng-Shan
Cao Ji-Chao
Zhang Jian
Zhang Xu-Long
Gao De-Min
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Abstract
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Thymopentin plays an important role in improving imbalanced immune systems of patients, however, it has a limited half-life in plasma. To get more stable and active thymopentin analogs, a fusion thymosin α1-thymopentin (Tα1-TP5) gene was synthesized and cloned into vector pGAPZαA. Tα1-TP5 fusion peptide was expressed in pichia pastoris and purified by metal chelating chromatography and gel filtration chromatography. The circular dichroism spectra (CD) indicated that the secondary structure of Tα1-TP5 fusion peptide is dominated by a-helix and random coil. In vitro analysis showed that the plasma half-life of Tα1-TP5 fusion peptide is 140 ±14 min, which is longer than that of TP5 (5.6±0.7 min) and Tα1 (127±11 min). The in vitro activity assay presented that Tα1-TP5 fusion peptide has greater activity in promoting proliferation of Kunming mouse splenocytes, and in vivo experiment it showed better activity in promoting the phagocytosis of macrophages and secretion of IL-2 than both Tα1 and TP5. Our findings suggest that Tα1-TP5 fusion peptide might be a potential therapeutic agent.
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KEYWORD
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Fusion peptide, Pichia pastoris, Thymopentin, Thymosin α1
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