Complexation of integral membrane proteins by phosphorylcholine-based amphipols.
Biochim Biophys Acta
; 1768(11): 2737-47, 2007 Nov.
Article
in En
| MEDLINE
| ID: mdl-17825785
ABSTRACT
Amphiphilic macromolecules, known as amphipols, have emerged as promising candidates to replace conventional detergents for handling integral membrane proteins in water due to the enhanced stability of protein/amphipol complexes as compared to protein/detergent complexes. The limited portfolio of amphipols currently available prompted us to develop amphipols bearing phosphorylcholine-based units (PC). Unlike carboxylated polymers, PC-amphipols remain soluble in aqueous media under conditions of low pH, high salt concentration, or in the presence of divalent ions. The solubilizing properties of four PC-amphipols were assessed in the case of two membrane proteins, cytochrome b(6)f and bacteriorhodopsin. The protein/PC-amphipol complexes had a low dispersity in size, as determined by rate zonal ultracentrifugation. Short PC-amphipols (
Search on Google
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Phosphorylcholine
/
Polymers
/
Detergents
/
Membrane Proteins
Language:
En
Journal:
Biochim Biophys Acta
Year:
2007
Document type:
Article
Affiliation country:
Canadá