Glycotripod Amphiphiles for Solubilization and Stabilization of a Membrane-Protein Superassembly: Importance of Branching in the Hydrophilic Portion

• Published in: Chembiochem : a European journal of chemical biology Vol. 9; no. 11; pp. 1706 - 1709
• Main Authors: Chae, Pil S, Wander, Marc J, Bowling, Aaron P, Laible, Philip D, Gellman, Samuel H
• Format: Journal Article
• Language: English
• Published: Weinheim Wiley-VCH Verlag 21.07.2008; WILEY-VCH Verlag; WILEY‐VCH Verlag
• Subjects: amphiphiles; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Carbohydrates - chemical synthesis; Carbohydrates - chemistry; Carbohydrates - pharmacology; Cell Membrane - chemistry; Cell Membrane - metabolism; detergent design; membrane proteins; Membrane Proteins - chemistry; Membrane Proteins - metabolism; Protein Binding - drug effects; Rhodobacter capsulatus - chemistry; Solubility - drug effects; solubilization; stabilization
• ISSN: 1439-4227; 1439-7633
• DOI: 10.1002/cbic.200800169

Three‐legged friends: Intrinsic membrane proteins must usually be extracted from the native membrane with the aid of synthetic amphiphiles and then stabilized before detailed structural and functional characterization is possible. We describe new amphiphiles with unusual architectures that were useful for extraction and stabilization of protein superassemblies from bacterial membranes. Our results suggest that incorporation of branch points (as shown in figure) in both the hydrophilic and lipophilic portions can lead to favorable amphiphile behavior.