Lipids regulate the structure and function of ion channels. While cryo-electron microscopy (cryo-EM) has recently revealed the structures of numerous lipid-bound ion channels, the mechanism by which lipids modulate these membranes is still poorly understood. Understanding the mechanism of lipid-ion channel interactions is a vital first step toward designing efficacious drug molecules. Pentameric ligand-gated ion channels (pLGICs) are lipid-sensitive channels that mediate synaptic signaling and regulate neuronal excitability and are drug targets for anesthetics and anti-epileptics. One technique used to identify lipid-ion channel binding sites includes quenching the fluorescence of tryptophan residues on a protein by brominated phospholipids. In the present study, we present our synthesis of three brominated phospholipids (brominated POPC, POPE, and POPG), as well as preliminary data to determine the identity of the phospholipid bound to the tryptophan residue W206 of the prokaryotic <i>Erwinia chrysanthemi</i> ligand-gated ion channel (ELIC).

Synthesis of brominated phospholipids for functional characterization of lipid-ion channel binding

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