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Ionic liquids as refolding additives: N'-alkyl and N'-(-hydroxyalkyl) N-methylimidazolium chlorides

Institut für Biotechnologie, Martin-Luther-Universität Halle/Wittenberg, 06120 Halle (Saale), Germany

(RECEIVED May 19, 2005; FINAL REVISION July 19, 2005; ACCEPTED July 19, 2005)

The purpose of this work was to investigate the influence of a series of N'-alkyl and N'-(-hydroxy-alkyl)-N-methylimidazolium chlorides on the renaturation of two model proteins, namely hen egg white lysozyme and the single-chain antibody fragment ScFvOx. All tested ionic liquids acted as refolding enhancers, with varying efficacies and efficiencies. The results of the refolding screening could be interpreted by taking into account the effect of the studied ionic liquids on protein aggregation, together with the systematic variations of their influence on the stability of native proteins in solution. More hydrophobic imidazolium cations carrying longer alkyl chains were increasingly destabilizing, while terminal hydroxylation of the alkyl chain made the salts more compatible with protein stability. The studied ionic liquids can be classified as preferentially bound, slightly to moderately chaotropic cosolvents for proteins.

Keywords: refolding; aggregation; stability; calorimetry; ionic liquids

Abbreviations: BSA, bovine serum albumin • DTT, dithiothreitol • GuHCl, guanidinium chloride • L-ArgHCl, L-arginine monohydro-chloride. Names of ionic liquids are abbreviated as indicated in Table 1.

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051596605.

Reprint requests to: Christian Lange, Institut für Biotechnologie, Martin-Luther-Universität Halle/Wittenberg, Kurt-Mothes-Str.3, 06120 Halle (Saale), Germany; e-mail: christian.lange{at}biochemtech.uni-halle.de; fax: +49-345-55-27013.

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