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Entropy-driven denaturation enables sustainable protein regeneration through rapid gel-solid transition
Yichong Wang1,2, Junlang Liu1, Michael M Peters2
1Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, USA.
Nature Communications
|July 27, 2025
Summary
Concentrated inorganic salts like lithium bromide (LiBr) denature proteins by disrupting water structure, not direct ion interaction. This enables efficient protein upcycling into biomaterials with closed-loop recycling.
Area of Science:
- Materials Science
- Biochemistry
- Physical Chemistry
Background:
- Protein upcycling is challenging due to difficulties in restructuring.
- Conventional methods use organic denaturants, complicating separation.
- Keratin treated with lithium bromide (LiBr) forms stable gels spontaneously.
Purpose of the Study:
- Investigate the denaturation mechanism of concentrated inorganic ion pairs on proteins.
- Understand the role of indirect solute effects in protein denaturation.
- Develop an efficient protein upcycling strategy.
Main Methods:
- Thermodynamic and spectroscopic analyses.
- Atomistic molecular simulations.
- Isolation of indirect solute effects.
Main Results:
- A universal, entropy-driven mechanism for salt-induced protein denaturation was identified.
- Concentrated ion pairs, such as LiBr, disrupt water network structure.
- This mechanism does not rely on direct protein-ion interactions.
Conclusions:
- Refined keratin extraction process allows spontaneous gel formation without extra chemicals.
- Achieved closed-loop recycling of the LiBr denaturant.
- Enabled versatile biomaterial production from protein resources through an effective strategy.
