Biomimetic Design of Membrane-active Amphiphilic Polymers

Abstract

The cell membrane is not only a cross-wall to compartmentalize cytoplasmic components but provides a functional interface for various biological pathways such as signal transduction, material transport, and energy production. Since these pivotal functions of cell membranes rely on the functional cooperation of a lipid bilayer and membrane proteins, it is essential to understand and control their interactions to develop novel membrane-targeting bioactive agents. In the molecular scale of view, membrane proteins or membrane-active peptides have an amphiphilic structure that is originated in the precise special arrangement of hydrophilic and hydrophobic amino acid residues. Based on the concept of biomimetics, we can develop novel biomaterials by employing synthetic molecular frameworks that display their function through the interaction with cell membranes by mimicking the nature of membrane proteins. In this article, the approach to design membrane-active amphiphilic polymers will be reviewed in comparison with natural proteins or peptides to be imitated. Membrane-active antimicrobial polymers have been designed by mimicking natural antimicrobial peptides that achieved high antimicrobial activity with low risk of resistance development and toxicity to host cells. Besides, an apolipoprotein-mimicking lipid nanodisc-forming polymer was developed toward the analysis of membrane proteins in an intact form.