Superchaotropic Stabilization of Monomeric Protein States

TL;DR

A boron cluster ion stabilizes proteins under heat and prevents them from clumping, which could help preserve protein function in storage.

Contribution

A superchaotrope stabilizes protein folding and inhibits interactions, offering a novel strategy for protein stabilization.

Findings

A boron cluster ion stabilizes protein folding under thermal stress.

It inhibits protein–protein interactions at millimolar concentrations.

Protein function is preserved in complex mixtures under ambient conditions.

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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