Expression of thymosin alpha1-thymopentin fusion peptide in Pichia pastoris and its characterization.
Gao. Demin D; Zhang. Xulong X; Zhang. Jian J; Cao. Jichao J; Wang. Fengshan F
Key Findings
- A fusion peptide (Talpha1âTP5) was successfully produced in yeast and purified.
- The fusion peptideâs plasma halfâlife (~140âŻmin) is much longer than thymopentin alone (â5âŻmin) and slightly longer than thymosinâalphaâ1 alone.
- In mouse tests, Talpha1âTP5 stimulated splenocyte growth, macrophage phagocytosis, and ILâ2 secretion better than either parent peptide.
Practical Outcomes
- While the study shows the fused peptide is more stable and immunologically active, itâs still an experimental biotech product not available for personal use. For biohackers, the takeaway is that linking thymosinâalphaâ1 with thymopentin may be a promising strategy for stronger, longerâlasting immune support, so keep an eye on future supplements or clinical trials that might commercialize this approach.
Summary
Scientists made a new protein that joins two immuneâboosting peptides (thymosinâalphaâ1 and thymopentin) together. This combined peptide lasts longer in the blood (about 2âŻhours) than each piece on its own and showed stronger effects on mouse immune cells, suggesting it could be a more powerful immuneâsupport tool.
Abstract
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 alpha1-thymopentin (Talpha1-TP5) gene was synthesized and cloned into vector pGAPZalphaA. Talpha1-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 Talpha1-TP5 fusion peptide is dominated by a-helix and random coil. In vitro analysis showed that the plasma half-life of Talpha1-TP5 fusion peptide is 140 +/- 14 min, which is longer than that of TP5 (5.6+/-0.7 min) and Talpha1 (127+/-11 min). The in vitro activity assay presented that Talpha1-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 Talpha1 and TP5. Our findings suggest that Talpha1-TP5 fusion peptide might be a potential therapeutic agent.
Study Information
pubmed
2008
2008-11-21T00:00:00.000Z
10.1007/s12272-001-2132-z
17
21