Zusammenfassung
Thermal imprinting of the lipid-water interface of phospholipid vesicles is achieved by reversible noncovalent assembly of membrane embedded amphiphilic metal complexes. The complexes have affinity to phosphate and imidazole groups and are preorganized by a phosphorylated hexapeptide template above the phase transition temperature. The template induced patterning is transferred into the gel phase ...
Zusammenfassung
Thermal imprinting of the lipid-water interface of phospholipid vesicles is achieved by reversible noncovalent assembly of membrane embedded amphiphilic metal complexes. The complexes have affinity to phosphate and imidazole groups and are preorganized by a phosphorylated hexapeptide template above the phase transition temperature. The template induced patterning is transferred into the gel phase of the membrane by cooling below the transition temperature. This limits the lateral
diffusion and stabilizes the metal complex receptor organization,
as confirmed by FRET measurements with dyelabeled receptors. After template removal an enhanced rebinding affinity of one order of magnitude for the target peptide was observed for the imprinted membranes compared to identical non-imprinted interfaces
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