Journal article
Amphipathic polymers: tools to fold integral membrane proteins to their active form



Publication Details
Authors:
Pocanschi, C.; Dahmane, T.; Gohon, Y.; Rappaport, F.; Apell, H.; Kleinschmidt, J.; Popot, J.
Publisher:
American Chemical Society
Publication year:
2006
Journal:
Biochemistry
Pages range:
13954-13961
Journal acronym:
Biochemistry
Volume number:
45
ISSN:
0006-2960
eISSN:
1520-4995

Abstract
Among the major obstacles to pharmacological and structural studies of integral membrane proteins (MPs) are their natural scarcity and the difficulty in overproducing them in their native form. MPs can be overexpressed in the non-native state as inclusion bodies, but inducing them to achieve their functional three-dimensional structure has proven to be a major challenge. We describe here the use of an amphipathic polymer, amphipol A8-35, as a novel environment that allows both beta-barrel and alpha-helical MPs to fold to their native state, in the absence of detergents or lipids. Amphipols, which are extremely mild surfactants, appear to favor the formation of native intramolecular protein-protein interactions over intermolecular or protein-surfactant ones. The feasibility of the approach is demonstrated using as models OmpA and FomA, two outer membrane proteins from the eubacteria Escherichia coli and Fusobacterium nucleatum, respectively, and bacteriorhodopsin, a light-driven proton pump from the plasma membrane of the archaebacterium Halobacterium salinarium.


Keywords
0 (Bacterial Outer Membrane Proteins), 0 (Escherichia coli Proteins), 0 (fomA protein, Fusobacterium), 0 (Membrane Proteins), 149024-69-1 (OMPA outer membrane proteins), 53026-44-1 (Bacteriorhodopsins), Bacterial Outer Membrane Proteins/chemistry, Bacteriorhodopsins/chemistry, Circular Dichroism, Escherichia coli Proteins/chemistry, Membrane Proteins/chemistry, Protein Folding, Spectrophotometry, Ultraviolet


Research Areas


Last updated on 2019-25-07 at 13:42