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Curr Opin Struct Biol. 2009 Aug;19(4):379-85. doi: 10.1016/j.sbi.2009.07.008. Epub 2009 Aug 12.

Lipopeptide detergents for membrane protein studies.

Author information

1
Ontario Cancer Institute, 101 College Street, Toronto, Ontario, Canada M5G 1L7. prive@uhnres.utoronto.ca

Abstract

An ideal detergent would be able to maintain a membrane protein in a soluble state with no measurable effect on the functional, structural, and thermodynamic properties of the protein relative to the bilayer-embedded state. Unfortunately, the detergents that are commonly used by membrane protein biochemists fall short of this standard. Although remarkable advances have been made in membrane protein structural biology, there remains a need for improved detergents that provide a more natural substitute for the membrane environment. Lipopeptide detergents (LPDs) are a new class of amphiphile designed to be better mimics of the bilayer at the hydrophobic surfaces of solubilized membrane proteins. LPDs consist of an alpha-helical peptide backbone that supports alkyl chains anchored at either end of the helix. The LPD monomers self-assemble into cylindrical micelles with a membrane-like packing of the inner core of alkyl chains.

PMID:
19682888
DOI:
10.1016/j.sbi.2009.07.008
[Indexed for MEDLINE]

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