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Ionic liquids as refolding additives: Variation of the anion

Paper ID Volume ID Publish Year Pages File Format Full-Text
24192 43504 2010 9 PDF Available
Title
Ionic liquids as refolding additives: Variation of the anion
Abstract

Several ionic liquids have been shown to act as suppressors of protein aggregation and to effectively promote the in vitro refolding of denatured proteins. In this work, the influence of the anion of these organic salts on their performance as refolding enhancers was tested, using a series of N-ethyl-N′-methyl imidazolium (EMIM) salts. Variation of the anion had a profound effect on the renaturation of the recombinant plasminogen activator rPA, which served as a model protein. The effect was roughly correlated with the stability of proteins in the tested aqueous ionic liquid solutions. Strongly destabilizing anions with higher alkyl substitutions like, e.g., hexyl sulfate were unable to promote protein refolding. However, the dimethyl and diethyl phosphate salts, which are known to be quite compatible with protein stability, also effectively suppressed renaturation, while alkylated sulfate anions with the same influence on protein stability did promote in vitro refolding. Only ionic liquid co-solvent systems with an intermediate capacity for solubilizing the proteinogenic amino acid tryptophan were found to permit effective renaturation of the model protein rPA. The most effective refolding enhancer among the tested ionic liquids was EMIM chloride.

Keywords
In vitro refolding; Protein stability; Ionic liquids; Recombinant plasminogen activator
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 150, Issue 1, 1 October 2010, Pages 64–72
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us