Lipid domain specific recruitment of lipophilic nucleic acids: a key for switchable functionalization of membranes.
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.
Institute of Biology/Biophysics, Humboldt-University Berlin, Invalidenstrasse 42, 10115 Berlin, Germany.
Martin
M
Loew
Ralph
R
Springer
Silvia
S
Scolari
Frank
F
Altenbrunn
Oliver
O
Seitz
Jürgen
J
Liebscher
Daniel
D
Huster
Andreas
A
Herrmann
Anna
A
Arbuzova
D000818:Animals; D004247:DNA / Q000737:chemistry*; D021962:Membrane Microdomains / Q000737:chemistry*; D008956:Models, Chemical; D020135:Peptide Nucleic Acids / Q000737:chemistry*
D020135:Peptide Nucleic Acids; D004247:DNA