Mimicking multipass transmembrane proteins: synthesis, assembly and folding of alternating amphiphilic multiblock molecules in liposomal membranes

摘要

Alternating amphiphilic multiblock molecules 1-4, involving fluorescent hydrophobic units, were designed as mimics for multipass transmembrane proteins. Fluorescence spectroscopy of 1-4 in liposomal membranes suggested the face-to-face stacking of the hydrophobic units to give folded structures as well as intermolecular assemblies. Synthetic molecules mimicking the structure and function of proteins have been attracting keen interest for development of molecular devices and medicines. Membrane proteins are important targets, where several synthetic ion channels, including tubes, ribbons, and barrels as mimics of P-barrel structures5 have been developed so far.