Self-Assembling and Ion Transport Properties of Membrane Active Peptides Driven by Formation of a Fluorous Interface

Abstract

Ion channel proteins are complex architectures vital for numerous physiological processes and involved in many diseases. With the aim of developing simpler supramolecular systems mimicking ion transport properties of channel proteins, we will describe novel helical peptides designed to self assemble in membranes into well defined superstructures capable of facilitating the translocation of ions. The driving force for self assembly is the formation of a stable fluorous interface created by interdigitation of fluorinated side chains of unnatural aminoacids incorporated at specific positions of the helical peptide. We will present the synthesis, the characterization and the ion transport abilities of a prototypical fluorinated peptide. We will also describe preliminary biophysical and computational studies done to delineate the membrane active structure.