NMR structure of human thymosin alpha-1.
Elizondo-Riojas. Miguel-Angel MA; Chamow. Steven M SM; Tuthill. Cynthia W CW; Gorenstein. David G DG; Volk. David E DE
Key Findings
- Thymosin‑alpha‑1 adopts a defined structure rather than being completely floppy
- Residues 14‑26 form an alpha‑helix
- The first 12 residues make two double β‑turns creating a distorted helical shape
Practical Outcomes
- Knowing the peptide’s stable regions can help hobbyists choose formulations that protect the helix (like using solvents or carriers that mimic the TFE/water mix) and may guide the design of more stable analogs, but it doesn’t change dosing or immediate usage instructions.
Summary
Scientists mapped the 3‑D shape of the 28‑amino‑acid peptide thymosin‑alpha‑1 and found it forms a stable helix in the middle part and two tight turns at the start. This tells us how the molecule folds, which can matter for how it works and how stable it is in the body.
Abstract
800 MHz NMR structure of the 28-residue peptide thymosin alpha-1 in 40% TFE/60% water (v/v) has been determined. Restrained molecular dynamic simulations with an explicit solvent box containing 40% TFE/60% TIP3P water (v/v) were used, in order to get the 3D model of the NMR structure. We found that the peptide adopts a structured conformation having two stable regions: an alpha-helix region from residues 14 to 26 and two double β-turns in the N-terminal twelve residues which form a distorted helical structure.
Study Information
pubmed
2011
2011-11-15T00:00:00.000Z
10.1016/j.bbrc.2011.11.041
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