Lipid domains in mammalian plasma membranes serve as platforms for specific recruitment or separation of proteins involved in various functions. Here, we have applied this natural strategy of lateral separation to functionalize lipid membranes at micrometer scale in a switchable and reversible manner. Membrane-anchored peptide nucleic acid and DNA, differing in their lipophilic moieties, partition into different lipid domains in model and biological membranes. Separation was visualized by hybridization with the respective complementary fluorescently labeled DNA strands. Upon heating, domains vanished, and both lipophilic nucleic acid structures intermixed with each other. Reformation of the lipid domains by cooling led again to separation of membrane-anchored nucleic acids. By linking appropriate structures/functions to complementary strands, this approach offers a reversible tool for triggering interactions among the structures and for the arrangement of reactions and signaling cascades on biomimetic surfaces.

Lipid anchors play an important biological role in natural proteins in particular in lipid membrane anchoring. This principle was extended to nonnatural nucleic acids, peptide nucleic acids (PNA) and peptides. In order to provide new lipophilic anchors for the introduction into peptide nucleic acids (PNA) or peptides, a number of new α-tocopherol derivatives were synthesized containing carboxylic acids, amino groups or alkyne groups as linking sites. Amongst them are compounds with one or with two tocopherol units. Sonogashira reaction turned out to be a useful tool in these approaches. The products were characterized by NMR-spectroscopy and MS. An unusual phenomenon was found in 2-propargylamino-4,6-difluorotriazine that exhibits two different chemical shifts in the 19 F-NMR spectrum for the two fluoro atoms.