Menu
Peptide Database
Results
No peptides found
Featured

Use search to browse all 100+ peptides

Thymosin-alpha-1

Thymalfasin, Zadaxin, Thymosin α1

Quick Stats
Studies 759
Trials 63
Score 2
2012 pubmed 11 citations

Intein-mediated expression, purification, and characterization of thymosin α1-thymopentin fusion peptide in Escherichia coli.

Li. Juan J; Zheng. Lei L; Li. Pingli P; Wang. Fengshan F

Key Findings

  • A self‑cleaving intein tag was used to express and purify Tα1‑TP5 in E. coli, reducing cost and steps.
  • The process yielded about 7.6 mg of 95% pure peptide per liter of culture after chromatography.
  • The purified Tα1‑TP5 stimulated proliferation of mouse splenic lymphocytes in vitro, confirming immune‑activating activity.

Practical Outcomes

  • The paper provides a blueprint for low‑cost, high‑purity production of Tα1‑TP5, which could be useful for biohackers with molecular biology capabilities. However, the method requires specialized lab equipment and expertise, so most enthusiasts may prefer purchasing the peptide. It also validates that the peptide has immune‑stimulating effects in cell tests.

Summary

Researchers figured out a cheap way to make a combined peptide called thymosin‑alpha‑1‑thymopentin (Tα1‑TP5) using bacteria. They got a decent amount of pure peptide and showed it can boost mouse immune cells in a dish. For DIYers, it shows the peptide can be produced in a lab, but you still need biotech skills and equipment.

Abstract

Thymosin α1-thymopentin (Tα1-TP5) fusion peptide has been proved to be an immune regulator based on its higher immunoregulatory activity than Tα1 and TP5. To obtain Tα1-TP5 more effectively and economically, Tα1-TP5 was genetically fused to a self-cleaving intein-chitin binding domain tag for purification via chitin beads in Escherichia coli. After affinity purification, the target peptide was released from the chitin beads via self-cleaving intein ((INTervening protEIN) induced by dithiothreitol. Further, Tα1-TP5 was purified by Superdex 30 and identified by Tricine-SDS-PAGE and electrospray ionization-mass spectrometry. Finally, about 7.6 mg Tα1-TP5 purified from the soluble fraction and inclusion bodies was obtained from 1 L culture media. The purity was 95% after a series of chromatographic purification steps. In vitro, the purified Tα1-TP5 could stimulate the proliferation of mouse splenic lymphocytes. Overall, this work demonstrated that Tα1-TP5 was purified with low cost and high efficiency, greatly expanding its potential use as an immune regulator.

Study Information

Provider

pubmed

Year

2012

Date

2012-04-25T00:00:00.000Z

DOI

10.1016/j.pep.2012.04.013

Citations

11

References

35