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Chemistry. 2013 Nov 11;19(46):15645-51. doi: 10.1002/chem.201301423. Epub 2013 Oct 2.

Novel tripod amphiphiles for membrane protein analysis.

Author information

1
Department of Bionano Engineering, Hanyang University Ansan, 426-791 (Korea), Fax: (+81) 31-436-8146. pchae@hanyang.ac.kr.

Abstract

Integral membrane proteins play central roles in controlling the flow of information and molecules across membranes. Our understanding of membrane protein structures and functions, however, is seriously limited, mainly due to difficulties in handling and analysing these proteins in aqueous solution. The use of a detergent or other amphipathic agents is required to overcome the intrinsic incompatibility between the large lipophilic surfaces displayed by the membrane proteins in their native forms and the polar solvent molecules. Here, we introduce new tripod amphiphiles displaying favourable behaviours toward several membrane protein systems, leading to an enhanced protein solubilisation and stabilisation compared to both conventional detergents and previously described tripod amphiphiles.

KEYWORDS:

amphiphiles; membrane proteins; molecular design; protein structures; stabilization

PMID:
24123610
PMCID:
PMC3947462
DOI:
10.1002/chem.201301423
[Indexed for MEDLINE]
Free PMC Article

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