Rationally-designed peptide anchor technology has been applied to the lipid bilayer interface in order to build ligand displays. In current work, we aim to employ alpha-helical peptides with integrated fluorophores as ligand anchoring molecules that are to span the lipid bilayer in a single pass.   We have used orthogonal side-chain modifications to add fluorophores and conjugation of the peptide termini allows access to a variety of chemistries or tethering or labeling purposes. We have synthesized core peptides with the target sequence K2A4L2A7L2A3K2-FITC followed by characterization via reversed phase HPLC in tandem with ESI-MS.  Conjugation of ligands at the peptide termini was carried out generally using hexahistidine chelation and also using biotinylation reagents in the proof of concept.The lateral fluidity and distribution of the fluorescently-tagged peptide within ligand displays supported on lipobeads was analyzed via confocal fluorescence imaging microscopy and was quantified using fluorescence recovery after photobleaching (FRAP) techniques

Alpha-helical peptide-based anchors in ligand displays

245th National Meeting (2013)

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