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. Keep the balance: Amphipathic agents are indispensable tools in membrane protein manipulation. New tripod amphiphiles (TPAs) were synthesised based on a detergent design principle from previously reported TPAs. The results show that the new agent "TPA-5-2" (see figure) confers an enhanced stability to a variety of membrane proteins relative to other TPAs and conventional detergents.
| Original language | English |
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| Journal | Chemistry: A European Journal |
| Volume | 19 |
| Issue number | 46 |
| ISSN | 0947-6539 |
| DOIs | |
| Publication status | Published - 11 Nov 2013 |