New tripod amphiphiles for membrane protein solubilization and stabilization

BIOL 66

Pil Seok Chae, pchae@wisc.edu1, Marc J. Wander, mwander@anl.gov2, Aaron P. Bowling2, Philip D. Laible2, and Samuel H. Gellman, gellman@chem.wisc.edu1. (1) Department of Chemistry, University of Wisconsin, 1101 University Avenue, Madison, WI 53706, (2) Biosciences Division, Argonne National Laboratory, 9700 South Cass Avenue, Argonne, IL 60439
Characterization of membrane proteins usually requires solubilization of the protein in aqueous media by use of a synthetic amphiphile. However, only a relatively limited range of amphiphile structures has been examined, and many membrane proteins are difficult to solubilize with available amphiphiles. Tripod amphiphiles were designed to overcome this limitation by exploration of new molecular backbones. These molecules are designed to display greater conformational stability than do conventional detergents, which may ultimately promote membrane protein crystallization. We will describe new types of tripod amphiphile that are very favorable for extraction of bacterial photosynthetic reaction center protein superassemblies from their native proteins.
 

Frontiers in Chemical Biology
5:00 PM-7:00 PM, Sunday, August 19, 2007 BCEC -- Exhibit Hall - B2, Poster

Division of Biological Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007