Membrane-anchored polyproline provides protein-like multimerization, controlled permeability and release from lipid vesicles

This study introduces the synthesis of a new class of lipopolymers, composed of L-proline monomer units and a phospholipid initiator. These lipopolymers were incorporated into lipid giant unilamelar vesicles and exhibited thermal hysteresis. Phase separation and polymer multimerization at the lipid bilayer was observed through confocal microscopy and confirmed by FRAP experiments. Such temperature-triggered membrane reorganiza-tion was accompanied by the release of probes up to 10 kDa, as monitored by fluorescence. These findings demonstrate that specifically engineered proline-based protein-like polymer functionalized by a phospholipid can display controlled self aggregation in phospholipid bilayer and localized stimuli responsive permeability.