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Issue 9, 2015
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Maltose neopentyl glycol-3 (MNG-3) analogues for membrane protein study

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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

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Supplementary files

Article information

04 Feb 2015
10 Mar 2015
First published
12 Mar 2015

Analyst, 2015,140, 3157-3163
Article type
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

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