Thymosin alpha-1 — pharmacology
Molecular targets, mechanism of action, pharmacokinetics and interactions as characterised in humans.
§2Pharmacology
§2.1Molecular targets
Table 2. Molecular targets recorded for Thymosin alpha-1, with the character of the interaction and the potency where the Institute holds it.
| Target | Interaction | Note |
|---|---|---|
| Toll-like receptor 9 and Toll-like receptor 2 | Reported agonist | Proposed mechanism for dendritic-cell and T-cell effects |
| T-lymphocyte maturation | Pleiotropic immunomodulation | Increases CD4 and CD8 counts and enhances antigen-specific responses in immunocompromised populations |
§2.2Mechanism of action
Thymosin alpha-1 promotes T-lymphocyte differentiation and maturation, increases interleukin-2 and interferon-gamma production, and enhances dendritic-cell function. Its clinical applications exploit immune reconstitution rather than direct antimicrobial or antineoplastic activity. Reported Toll-like receptor engagement provides a molecular mechanism, though the pleiotropy of the observed effects exceeds what a single receptor interaction readily explains.[1,2]
§2.3Pharmacokinetics
- Terminal half-life
- ≈2 h
- Time to maximum concentration
- ≈1–2 h after subcutaneous administration
- Volume of distribution
- not extensively distributed
- Plasma protein binding
- not extensively bound
- Clearance
- not published
- Bioavailability
- well absorbed subcutaneously
Proteolytic degradation. Endogenous thymosin alpha-1 is present in plasma, complicating pharmacokinetic interpretation.
§2.4Interactions
- Immunosuppressants — pharmacodynamic antagonism
References cited on this page
References are numbered in order of first citation in this document. Each superscript in the text links to its entry below.
- Garaci E, Pica F, Serafino A, Balestrieri E, Matteucci C, Moroni G, Sorrentino R, Zonfrillo M, Pierimarchi P, Sinibaldi-Vallebona P. Thymosin α1 and cancer: action on immune effector and tumor target cells. Annals of the New York Academy of Sciences 2007;1112:225–234. doi:10.1196/annals.1415.025 · PMID 17567944
- D’Hondt M, Bracke N, Taevernier L, Gevaert B, Verbeke F, Wynendaele E, De Spiegeleer B. Related impurities in peptide medicines. Journal of Pharmaceutical and Biomedical Analysis 2014;101:2–30. doi:10.1016/j.jpba.2014.06.012 · PMID 25044089
Identifiers are reproduced only where the Institute holds them. Where a digital object identifier or PubMed identifier is not shown, the Institute has recorded the journal and year and has not constructed an identifier.