2. Academic Validation
  3. Superchaotropic Stabilization of Monomeric Protein States

Superchaotropic Stabilization of Monomeric Protein States

  • Biomacromolecules. 2025 Aug 31. doi: 10.1021/acs.biomac.5c00944.
Ben Tin Yan Wong 1 2 3,  Lichun Zhang 1 2 3,  Thomas Chun Yip Wong 2 3,  Chun Ngo Yau 3,  Adrian Jun Chu 4,  Tsz Fung Tsang 4,  Joshua Jing Xi Li 5,  Xiao Yang 4,  Hei Ming Lai 1 2 3 6
Affiliations

Affiliations

  • 1 Department of Chemical Pathology, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, Hong Kong SAR, China.
  • 2 Illumos Limited, Hong Kong Science and Technology Park, Shatin, Hong Kong SAR, China.
  • 3 Li Ka Shing Institute of Health Sciences, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, Hong Kong SAR, China.
  • 4 Department of Microbiology, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, Hong Kong SAR China.
  • 5 Department of Pathology, School of Clinical Medicine, The University of Hong Kong, Queen Mary Hospital, Pok Fu Lam, Hong Kong SAR, China.
  • 6 Department of Psychiatry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, Hong Kong SAR, China.
PMID: 40887766 DOI: 10.1021/acs.biomac.5c00944
Abstract

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.

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