Novel tripod amphiphiles for membrane protein analysis

Pil Seok Chae, Andrew C Kruse, Kamil Gotfryd, Rohini R. Rana, Kyung Ho Cho, Søren G F Rasmussen, Hyoung Eun Bae, Richa Chandra, Ulrik Gether, Lan Guan, Brian K. Kobilka, Claus J. Loland, Bernadette Byrne, Samuel H. Gellman

Research output: Contribution to journalArticleResearchpeer-review

43 Citations (Scopus)


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 languageEnglish
Pages (from-to)15645-15651
Number of pages7
JournalChemistry - A European Journal
Issue number46
Publication statusPublished - 11 Nov 2013
Externally publishedYes


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

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