Issue 9, 2015

Maltose neopentyl glycol-3 (MNG-3) analogues for membrane protein study

Abstract

Detergents are typically used to both extract membrane proteins (MPs) from the lipid bilayers and maintain them in solution. However, MPs encapsulated in detergent micelles are often prone to denaturation and aggregation. Thus, the development of novel agents with enhanced stabilization characteristics is necessary to advance MP research. Maltose neopentyl glycol-3 (MNG-3) has contributed to >10 crystal structures including G-protein coupled receptors. Here, we prepared MNG-3 analogues and characterised their properties using selected MPs. Most MNGs were superior to a conventional detergent, n-dodecyl-β-D-maltopyranoside (DDM), in terms of membrane protein stabilization efficacy. Interestingly, optimal stabilization was achieved with different MNG-3 analogues depending on the target MP. The origin for such detergent specificity could be explained by a novel concept: compatibility between detergent hydrophobicity and MP tendency to denature and aggregate. This set of MNGs represents viable alternatives to currently available detergents for handling MPs, and can be also used as tools to estimate MP sensitivity to denaturation and aggregation.

Graphical abstract: Maltose neopentyl glycol-3 (MNG-3) analogues for membrane protein study

Supplementary files

Article information

Article type
Paper
Submitted
04 Feb 2015
Accepted
10 Mar 2015
First published
12 Mar 2015

Analyst, 2015,140, 3157-3163

Author version available

Maltose neopentyl glycol-3 (MNG-3) analogues for membrane protein study

K. H. Cho, M. Husri, A. Amin, K. Gotfryd, H. J. Lee, J. Go, J. W. Kim, C. J. Loland, L. Guan, B. Byrne and P. S. Chae, Analyst, 2015, 140, 3157 DOI: 10.1039/C5AN00240K

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