Superchaotropic Stabilization of Monomeric Protein States
Chaotropes are long known to destabilize protein assemblies and folding. We report that a boron cluster ion, as a weakly coordinating superchaotrope, can paradoxically stabilize protein folding even under extended thermal stresses while broadly inhibiting specific and nonspecific protein-protein interactions at millimolar concentrations for multiple proteins. Thermodynamic and kinetic investigations suggest that the boron cluster ion reduced the association rates of protein association and rendered protein-associative interactions entropically unfavorable. The preliminary utility of this phenomenon is demonstrated by the preservation of protein functions within complex mixtures stored in ambient, uncontrolled conditions, boosting their shelf life and stability against aggregation.
Authors
- Tsz Fung Tsang (ORCID: https://orcid.org/0000-0001-7904-277X)
- Joshua Li (ORCID: https://orcid.org/0000-0003-2425-0314)
- Xiao Yang (ORCID: https://orcid.org/0000-0002-3071-6531)
- Adrian Jun Chu (ORCID: https://orcid.org/0000-0001-9206-9395)
- Chun Ngo Yau (ORCID: https://orcid.org/0000-0002-1450-626X)
- H. M. Lai (ORCID: https://orcid.org/0000-0001-5150-7918)
- Liang Zhang (ORCID: https://orcid.org/0000-0002-8338-784X)
- Ben Tin Yan Wong
- Thomas Chun Yip Wong
Institutions
- Chinese University of Hong Kong (HK)
- Queen Mary Hospital (CN)
- Hong Kong Science and Technology Parks Corporation (HK)
- University of Hong Kong (HK)
Publication Details
- Journal
- Biomacromolecules
- Published
- 2025-09-01
- DOI
- https://doi.org/10.1021/acs.biomac.5c00944
- Primary Topic
- Spectroscopy and Quantum Chemical Studies
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Queen Mary University of London
- Croucher Foundation
- University of Hong Kong
- Chinese University of Hong Kong