Issue 11, 2017

Can an ammonium-based room temperature ionic liquid counteract the urea-induced denaturation of a small peptide?

Abstract

The folding/unfolding equilibrium of proteins in aqueous medium can be altered by adding small organic molecules generally termed as co-solvents. Denaturants such as urea are instrumental in the unfolding of proteins while protecting osmolytes favour the folded ensemble. Recently, room temperature ionic liquids (ILs) have been shown to counteract the deleterious effect of urea on proteins. In this paper, using atomistic molecular dynamics we show that a ternary mixture containing a particular ammonium-based IL, triethylammonium acetate (TEAA), and urea (in 1 : 5 molar ratio) helps a small 15-residue S-peptide analogue regain most of its native structure, whereas a binary aqueous mixture containing a large amount of urea alone completely distorts it. Our simulations show that the denaturant urea directly interacts with the peptide backbone in the binary mixture while for the ternary mixture both urea as well as the IL are preferentially excluded from the peptide surface.

Graphical abstract: Can an ammonium-based room temperature ionic liquid counteract the urea-induced denaturation of a small peptide?

Supplementary files

Article information

Article type
Paper
Submitted
27 12 2016
Accepted
22 2 2017
First published
22 2 2017

Phys. Chem. Chem. Phys., 2017,19, 7772-7787

Can an ammonium-based room temperature ionic liquid counteract the urea-induced denaturation of a small peptide?

S. Ghosh, S. Dey, M. Patel and R. Chakrabarti, Phys. Chem. Chem. Phys., 2017, 19, 7772 DOI: 10.1039/C6CP08842B

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