(464b) An Engineered Platform for High-Throughput Characterization of Peptide Binding to Membranes

A common motif amongst peripheral membrane-binding proteins is a disordered polypeptide domain that can be induced into an amphipathic helix (whereby polar and hydrophobic residues segregate to opposing helix surfaces) with a cognate membrane, thereby controlling protein subcellular localization. However, these peptides are often difficult to characterize in isolate, as they are prone to aggregation and methods to measure binding are low throughput. Herein, we present an engineered platform to enable high-throughput characterization of peptide binding to membranes via fluorescence anisotropy that has been cross-validated with corresponding tryptophan fluorescence measurements. These results represent the first steps in a highly scalable program to not only understand the ability of peptides to detect membrane composition but synthesize novel motifs for subcellular localization of therapeutics.