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OmpA Membrane Domain as a Tight‐Binding Anchor for Lipid Bilayers
Author(s) -
Ringler Philippe,
Schulz Georg E.
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20020503)3:5<463::aid-cbic463>3.0.co;2-p
Subject(s) - biotinylation , lipid bilayer , streptavidin , biophysics , chemistry , liposome , membrane , biotin , cysteine , membrane protein , protein–lipid interaction , bilayer , biochemistry , integral membrane protein , biology , enzyme
A β‐barrel anchor was engineered as a new tool for specific and reversible attachment of liposomes to surfaces. A single cysteine residue (Cys 26) was introduced at a mobile extracellular loop of the depicted integral membrane protein OmpA and labeled with biotin. The binding of streptavidin to the biotinylated OmpA protein was characterized in the presence of detergent and after reconstitution in proteoliposomes. The protein anchor OmpA holds a lipid bilayer much more tightly than a lipid‐based anchor and OmpA is evenly dispersed in the membrane.