Journal of the American Chemical Society · 2009 · 34 citations · 15 references
Life SciencesBiochemistryMolecular BiologyLipid BiochemistryMembrane BiochemistryMembrane BiophysicsBiological MembranesMembrane DomainsMembrane EngineeringMembrane MicrodomainsMembrane ProteinsMembrane Self-assemblyMembrane Domain AssemblyMembrane Lipid Domain OrganizationMembrane Protein AssemblyMembrane Protein ReconstitutionMembrane Targeting By Lipid BindingModel Membrane SystemsProtein-mediated Membrane Assembly
Lipid membranes composed of an iminodiacetic acid functionalized lipid, DSIDA, in a POPC matrix exhibited switchable properties via Cu(2+) recognition to rapidly assemble microdomains that act as high affinity sites for His-tagged proteins. The microdomains demonstrated an order of magnitude enhanced affinity for the proteins compared to homogeneously functionalized POPC membranes with Ni(2+)-NTA DOGS or Cu(2+)-DOIDA, while a rapid release and restoration of the original membrane was accomplished with micromolar concentrations of EDTA.
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