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 pro 2016
Accepted
22 vlj 2017
First published
22 vlj 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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements