A multipass transmembrane (MTM) structure is prevalent in membrane proteins for a wide range of functions. Typically, the MTM structure is constructed of bundled multiple α-helices spanning the membrane which are connected by flexible domains. One characteristic feature of MTM proteins is dynamic functions such as stimuli responses and conformational changes. In this review, the development of synthetic molecules forming an MTM structure in membranes is highlighted. The MTM folded structure is developed using an amphiphilic molecular design with a multiblock strategy between rigid hydrophobic components and flexible hydrophilic units. Such synthetic amphiphiles not only form the MTM structure by folding but also self-assemble to construct supramolecular ion channels. An elaborated molecular design of the MTM structure with a ligand-binding pocket allows for ligand-gated regulation of ion transport. Light-triggered membrane deformation for vesicle budding is also demonstrated.
Keywords: foldamer; ion channel; membrane protein; multipass transmembrane structure; self-assembly; vesicle budding.