Structural properties of soluble peptide amphiphile micelles

Abstract

Peptide amphiphiles (PAs) self-assemble into dynamic micellar structures that provide a multivalent display of functional peptides and are currently being developed for use in a wide range of therapeutic and diagnostic applications. This review focuses on the physical properties of PA assemblies that remain soluble under physiological conditions, termed protein analogous micelles. The relationship between PA monomer design, secondary structure, and the resulting micelle size and shape is examined, highlighting the complex balance of forces between the hydrophobic tail and the peptide headgroup. Micelle stability is also discussed, as stability is an important factor which will dictate the circulation behavior of micelles and their interaction with various tissues and cells. Analysis of different PA systems reveals methods for controlling micelle structure and stability, demonstrating how the physical properties of PA micelles can be tailored for specific applications.