Rigid Amphiphiles for Membrane Protein Manipulation

✍ Scribed by D. Tyler McQuade; Mariah A. Quinn; Seungju M. Yu; Arthur S. Polans; Mark P. Krebs; Samuel H. Gellman

• Book ID: 101307045
• Publisher: John Wiley and Sons
• Year: 2000
• Tongue: English
• Weight: 98 KB
• Volume: 112
• Category: Article
• ISSN: 0044-8249
• DOI: 10.1002/(sici)1521-3757(20000218)112:4<774::aid-ange774>3.0.co;2-w

✦ Synopsis

The shape of an amphiphile strongly influences selfassociation in solution [1] and in liquid crystalline phases, [2] as well as interactions with self-assembled structures such as lipid bilayers. [3] In recent years several groups have examined unusual amphiphile topologies. [4, 5] We and others, for example, have explored amphiphiles in which hydrophilic groups project on one side of an approximately planar hydrophobic unit (ªcontrafacial amphiphilesº). [4] Here we introduce a related family of molecules based on a rigid quaternary carbon center, ªtripod amphiphilesº (A), and present evidence that these amphiphiles can solubilize the two nonhomologous membrane proteins bacteriorhodopsin (BR) and bovine rhodopsin (Rho) in a stable monomeric state.