Issue 42, 2014

New ganglio-tripod amphiphiles (TPAs) for membrane protein solubilization and stabilization: implications for detergent structure–property relationships

Abstract

Detergents are widely used for membrane protein research; however, membrane proteins encapsulated in micelles formed by conventional detergents tend to undergo structural degradation, necessitating the development of new agents with enhanced efficacy. Here we prepared several hydrophobic variants of ganglio-tripod amphiphiles (TPAs) derived from previously reported TPAs and evaluated for a multi-subunit, pigment protein superassembly. In this study, TPA-16 was found to be most efficient in protein solubilization while TPA-15 proved most favourable in long-term protein stability. The current study combined with previous TPA studies enabled us to elaborate on a few detergent structure–property relationships that could provide useful guidelines for novel amphiphile design.

Graphical abstract: New ganglio-tripod amphiphiles (TPAs) for membrane protein solubilization and stabilization: implications for detergent structure–property relationships

Supplementary files

Article information

Article type
Paper
Submitted
02 Jul 2014
Accepted
26 Aug 2014
First published
26 Aug 2014

Org. Biomol. Chem., 2014,12, 8480-8487

Author version available

New ganglio-tripod amphiphiles (TPAs) for membrane protein solubilization and stabilization: implications for detergent structure–property relationships

P. S. Chae, H. E. Bae, M. Ehsan, H. Hussain and J. W. Kim, Org. Biomol. Chem., 2014, 12, 8480 DOI: 10.1039/C4OB01375A

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