Issue 13, 2018

Local chemistry of the surfactant's head groups determines protein stability in reverse micelles

Abstract

When comparing protein folding in vitro and in vivo significant differences have been found. This has been attributed to crowding and confinement effects. Using a combination of GHz- and THz-dielectric relaxation spectroscopy and MD simulations, we studied hydration dynamics and reviewed protein stability data inside sodium bis(2-ethylhexyl)sulfosuccinate (AOT) and cetyltrimethylammonium bromide (CTAB) reverse micelles which are model systems for confinement. We find that water inside anionic AOT and cationic CTAB reverse micelles is characterized by a strong dielectric depolarization giving rise to a very low relative permittivity compared to an unconfined solution. Despite differences in the hydration dynamics of the surfactant's head groups, simulations using the two-phase thermodynamics method predict a similar reduction in water entropy for both reverse micelle systems compared to bulk water. When we compare the stability data of proteins in these reverse micelles we find that in contrast to our initial expectation, protein stability correlates rather with the local chemistry of the hydrated head groups than with the excluded volume effect or the low global permittivity.

Graphical abstract: Local chemistry of the surfactant's head groups determines protein stability in reverse micelles

Supplementary files

Article information

Article type
Paper
Submitted
18 jan 2018
Accepted
22 feb 2018
First published
27 feb 2018

Phys. Chem. Chem. Phys., 2018,20, 8515-8522

Local chemistry of the surfactant's head groups determines protein stability in reverse micelles

M. Senske, Y. Xu, A. Bäumer, S. Schäfer, H. Wirtz, J. Savolainen, H. Weingärtner and M. Havenith, Phys. Chem. Chem. Phys., 2018, 20, 8515 DOI: 10.1039/C8CP00407B

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