Аннотация:Cell membranes play a key role in bottom-up synthetic biology, as they enableinteraction control, transport, and other essential functions. These ultra-thin,flexible, yet stable structures form through the self-assembly of lipids andproteins. While liposomes are common mimics, their synthetic membranesoften fail to replicate natural properties due to poor structural control. Toaddress this, pepticombs are introduced, a new family of supramolecularbuilding blocks. They are synthesized by regularly appending anionicsurfactants with lipid-long alkyl tails to cationic amino acid residues ofrecombinant elastin-like supercharged unfolded polypeptides (SUPs). Usingmicroscopy techniques and molecular dynamics simulations, the formation ofgiant unilamellar vesicles, termed pepticombisomes, is demonstrated andtheir membrane properties are characterized. The molecular topology ofpepticombs allows for precise mimicry of membrane thickness and flexibility,beyond classic polymersomes. Unlike the previously introducedionically-linked comb polymers, all pepticombs exhibit a uniform degree ofpolymerization, composition, sequence, and spontaneous curvature. Thisuniformity ensures consistent hydrophobic tail distribution, facilitatingintermolecular hydrogen bonding within the backbone. This generates elasticheterogeneities and the concomitant formation of non-icosahedral facetedvesicles, as previously predicted. Additionally, pepticombisomes canincorporate functional lipids, enhancing design flexibility