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Thymosin-alpha-1

Thymalfasin, Zadaxin, Thymosin α1

Quick Stats
Studies 759
Trials 63
Score 3
2010 pubmed 21 citations

Bioactivity and pharmacokinetics of two human serum albumin-thymosin alpha1-fusion proteins, rHSA-Talpha1 and rHSA-L-Talpha1, expressed in recombinant Pichia pastoris.

Chen. Jian-Hua JH; Zhang. Xin-Guo XG; Jiang. Yu-Tao YT; Yan. Lu-Ying LY; Tang. Li L; Yin. Yi-Wei YW; Cheng. Dai-Shuang DS; Chen. Jing J; Wang. Min M

Key Findings

  • Fusing thymosin‑alpha‑1 to human serum albumin (with or without a short linker) yields a highly pure protein (>97%).
  • Both fusion proteins enhance T‑cell maturation and protect thymocytes from dexamethasone‑induced death in vitro.
  • In mice, daily sub‑cutaneous injections for a week improve body weight, spleen and thymus indices, increase plasma SOD (antioxidant) and lower MDA (oxidative stress).
  • Pharmacokinetic testing in rats shows a markedly prolonged half‑life versus native thymosin‑alpha‑1.

Practical Outcomes

  • For biohackers, the main takeaway is that attaching thymosin‑alpha‑1 to a large carrier like albumin can dramatically extend its circulation time, potentially allowing less frequent dosing while retaining immune‑boosting effects. While the fusion proteins are still experimental and not commercially available, the data suggest that future long‑acting thymosin‑alpha‑1 formulations could be more convenient and effective for immune support, viral protection, or anti‑aging protocols.

Summary

Scientists linked thymosin‑alpha‑1 (a peptide that can boost immune function) to human serum albumin, creating two new fusion proteins that stay in the body much longer and still work to support immune cells in mice. The study shows these hybrids improve weight gain, spleen and thymus health, and antioxidant markers compared to the plain peptide.

Abstract

Thymosin-alpha1 (Talpha1) is indicated for the treatment of certain viral infections, including hepatitis B and C, and cancers, such as melanoma. In this paper, the fusion genes encoding human serum albumin (HSA) and Talpha1 with (rHSA-L-Talpha1) and without a linker peptide (rHSA-Talpha1) were constructed and overexpressed in P. pastoris. Through the process of ion interaction chromatography (Q-Sepharose F.F), hydrophobic interaction chromatography (Phenyl Sepharose HP) and affinity chromatography (Blue Sepharose F.F), the purity of fusion proteins was greater than 97%. In contrast to the reactivity of normal spleen cells to Con A, the data of in vitro murine spleen lymphocytes proliferation experiment suggested that spleen cells achieved a higher degree of T cell maturation after rHSA-L-Talpha1, rHSA-Talpha1 and Talpha1 treatments, respectively. Moreover, rHSA-L-Talpha1, rHSA-Talpha1 and Talpha1 can also antagonize dexamethasone-induced apoptosis of thymocyte sub-populations. In hydrocortisone-induced immunosuppression mice (in vivo experiments), after subcutaneous injections with two fusion proteins and Talpha1 for seven consecutive days, the net increment of body weight, the spleen index and the thymus index were significantly improved. Simultaneously, the increase in SOD level and the decrease in MDA level in plasma were observed. The pharmacokinetic data of rHSA-L-Talpha1 and rHSA-Talpha1 administered in rats showed an improved pharmacokinetic profile with a conspicuous prolonged half life. The analysis of bioactivity and pharmacokinetics suggested that fusion proteins rHSA-L-Talpha1 and rHSA-Talpha1 were new drug candidates.

Study Information

Provider

pubmed

Year

2010

Date

2010-05-16T00:00:00.000Z

DOI

10.1007/s00262-010-0862-9

Citations

21

References

45