In situ Synthesis of Lipopeptides as Versatile Receptors for the Specific Binding of Nanoparticles and Liposomes to Solid-Supported Membranes

A detailed study of the in situ coupling of small peptides such as CGGH6 (H6) and CGWK8 (K8) to maleimide functionalized phospholipid bilayers is presented. Individually addressable microstructured membranes are employed to unequivocally probe the conjugation. The in situ coupling of peptides via a terminal cysteine moiety to maleimide functionalized phospholipids is shown to be a convenient and versatile way to selectively fabricate peptide‐modified phospholipid bilayers serving as specific receptor platforms for functionalized vesicles and nanoparticles. Specific binding of functional vesicles to the peptide‐modified bilayers is achieved by either histidine complexation with Ni‐NTA‐DOGS containing vesicles or electrostatic interaction between positively charged oligolysine bearing lipopeptides and negatively charged POPC/POPG vesicles. Peptide receptors are also found to be easily accessible from the aqueous phase and not buried within the membrane interior. In situ lipopeptide synthesis on solid‐supported lipid membranes (see image) is introduced and the ability to serve as receptor structures is evaluated. The interaction of functionalized vesicles is found to occur exclusively on peptides displaying maleimide‐functionalized lipid bilayers.