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Issue 2, 2012
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How ionic liquids can help to stabilize native proteins

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The native state of a globular protein is essential for its biocatalytic function, but is marginally stable against unfolding. While unfolding equilibria are often reversible, folding intermediates and misfolds can promote irreversible protein aggregation into amorphous precipitates or highly ordered amyloid states. Addition of ionic liquids—low-melting organic salts—offers intriguing prospects for stabilizing native proteins and their enzymatic function against these deactivating reaction channels. The huge number of cations and anions that form ionic liquids allows fine-tuning of their solvent properties, which offers robust and efficient strategies for solvent optimization. Going beyond case-by-case studies, this article aims at discussing principles for a rational design of ionic liquid-based formulations in protein chemistry and biocatalysis.

Graphical abstract: How ionic liquids can help to stabilize native proteins

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The article was received on 15 Jun 2011, accepted on 26 Oct 2011 and first published on 16 Nov 2011

Article type: Perspective
DOI: 10.1039/C1CP21947B
Phys. Chem. Chem. Phys., 2012,14, 415-426

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    How ionic liquids can help to stabilize native proteins

    H. Weingärtner, C. Cabrele and C. Herrmann, Phys. Chem. Chem. Phys., 2012, 14, 415
    DOI: 10.1039/C1CP21947B

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