Principal Investigator Shuguang Zhang
Membrane proteins play vital roles in every aspect of cellular activities. In order to study diverse membrane proteins, it is crucial to select the right surfactants to stabilize them for analysis. Despite much effort, little progress has been made to elucidate their structure and function, largely due to lack of suitable surfactants. Here we report stabilization of a G-protein coupled receptor bovine rhodopsin in solution using a new class of designer short and simple peptides surfactants. These surfactants consist of seven amino acids with a hydrophilic head, aspartic acid or lysine, and a hydrophobic tail with six consecutive alanines. These peptide surfactants not only enhance the stability of bovine rhodopsin in the presence of lipids and common surfactants n-Dodecyl-≤-D-maltoside (DM) and octyl-D-glucoside (OG), but they also significantly stabilize rhodopsin under thermal denaturation conditions, even after lipids were removed. These peptide surfactants are simple, versatile, effective, and affordable. They represent a new designer molecular nanomaterial for use in studies of diverse elusive membrane proteins.