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Thymosin-alpha-1

Thymalfasin, Zadaxin, Thymosin α1

Quick Stats
Studies 759
Trials 63
Score 3
2008 pubmed 17 citations

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 (Talpha1‑TP5) was successfully produced in yeast and purified.
  • The fusion peptide’s plasma half‑life (~140 min) is much longer than thymopentin alone (≈5 min) and slightly longer than thymosin‑alpha‑1 alone.
  • In mouse tests, Talpha1‑TP5 stimulated splenocyte growth, macrophage phagocytosis, and IL‑2 secretion better than either parent peptide.

Practical Outcomes

  • While the study shows the fused peptide is more stable and immunologically active, it’s still an experimental biotech product not available for personal use. For biohackers, the takeaway is that linking thymosin‑alpha‑1 with thymopentin may be a promising strategy for stronger, longer‑lasting 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 immune‑boosting peptides (thymosin‑alpha‑1 and thymopentin) together. This combined peptide lasts longer in the blood (about 2 hours) than each piece on its own and showed stronger effects on mouse immune cells, suggesting it could be a more powerful immune‑support 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

Provider

pubmed

Year

2008

Date

2008-11-21T00:00:00.000Z

DOI

10.1007/s12272-001-2132-z

Citations

17

References

21