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A temperature-triggered phase separation system for stabilizing bioactive protein structure and function.

Yanan Wei1, Zhijie Li1, Fan Ni1

  • 1Department of Chemistry, College of Sciences, Northeastern University, Shenyang, 110819, China.

Talanta
|March 26, 2026
PubMed
Summary
This summary is machine-generated.

This study introduces a novel heat-shock-activated system to protect sensitive protein pharmaceuticals from cold chain damage. The reversible water-in-water system shields proteins during storage and transport, maintaining their biological function.

Keywords:
Aqueous two-phase systemIonic liquidPhase separationProtein aggregationProtein protection

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Area of Science:

  • Biotechnology
  • Materials Science
  • Pharmaceutical Sciences

Background:

  • Protein-based drugs like vaccines are vulnerable to aggregation and denaturation from temperature changes during storage and transport.
  • Current cold chain methods are insufficient to prevent structural damage, compromising drug efficacy.

Purpose of the Study:

  • To develop a heat-shock-triggered, reversible water-in-water (W/W) protein shielding system.
  • To create a system with a tunable activation temperature for protecting proteins against cold chain failures.

Main Methods:

  • A W/W system utilizing polypropylene glycol (PPG) and ionic liquids (ILs) was designed with a 10°C cloud point.
  • The system undergoes phase separation upon exceeding the cloud point, encapsulating and stabilizing proteins.
  • Two protective systems (PPG30/ChCl16 and PPG30/TCC12) were tested for protein protection.

Main Results:

  • The system effectively protected a wide range of proteins from thermal stress.
  • Enzymatic activity of lipase and β-galactosidase remained largely intact after multiple heating cycles.
  • The protein-containing phase was easily retrievable via centrifugation after system use.

Conclusions:

  • This heat-shock-responsive W/W system offers a facile and effective method for protecting proteins.
  • The technology provides on-demand protection against thermal and mechanical stresses for ambient storage and transport.
  • This approach enhances the stability and shelf-life of protein-based pharmaceuticals.