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Zinc Coordination by Thymosin β4: Structural Determinants and Functional Implications.

Joanna Izabela Lachowicz¹, Terenzio Congiu², Andrea Salis³

¹Department of Environmental Health, Occupational Medicine and Epidemiology, Wroclaw Medical University, Mikulicza-Radeckiego 7, 50-368 Wroclaw, PL, Poland.

International Journal of Molecular Sciences

|February 27, 2026

Summary

Thymosin β4 (Tβ4) binds Zn²⁺, forming complexes and aggregating under physiological conditions. This Zn(II)-induced aggregation may impact Tβ4 function in specific microdomains with high zinc levels.

Keywords:

electrospray ionization mass spectrometry (ESI-MS)scanning electron microscopy (SEM)thymosin β4 (Tβ4)zinc (Zn)

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Published on: May 13, 2020

Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

Thymosin β4 (Tβ4) is a peptide with diverse biological roles.
Its interactions with metal ions, particularly Zn²⁺, are not well understood.
Understanding these interactions is crucial for elucidating Tβ4's function.

Purpose of the Study:

To investigate the interaction between Thymosin β4 (Tβ4) and Zn²⁺ ions.
To determine if Zn²⁺ binding induces structural changes or aggregation in Tβ4.
To assess the physiological relevance of Tβ4/Zn²⁺ interactions.

Main Methods:

Zeta potential analysis
Dynamic light scattering (DLS)
Electrospray ionization mass spectrometry (ESI-MS)
Nuclear magnetic resonance (NMR) spectroscopy
Scanning electron microscopy with elemental mapping (SEM/EDS)

Main Results:

Tβ4 forms discrete Zn²⁺-bound adducts and aggregates under physiological pH.
Zn(II) binding neutralizes Tβ4's negative charge, triggering aggregation.
ESI-MS identified Tβ4/Zn(II) complexes with a 1:3 molar ratio; DLS and SEM showed compact assemblies.
NMR confirmed Zn(II)-induced aggregation without Tβ4 folding.

Conclusions:

Zn(II)-induced aggregation of Tβ4 is feasible in zinc-rich microdomains (e.g., synaptic cleft), but unlikely in plasma.
This Zn(II)-mediated supramolecular assembly could influence Tβ4 behavior in neurological and inflammatory conditions.
Establishes a biochemical framework for studying Tβ4/Zn(II) complexation in vivo.