Review self‐assembly of amphipathic β‐sheet peptides: Insights and applications

Abstract

Amphipathic peptides composed of alternating polar and nonpolar residues have a strong tendency to self‐assemble into one‐dimensional, amyloid‐like fibril structures. Fibrils derived from peptides of general (XZXZ)n sequence in which X is hydrophobic and Z is hydrophilic adopt a putative β‐sheet bilayer. The bilayer configuration allows burial of the hydrophobic X side chain groups in the core of the fibril and leaves the polar Z side chains exposed to solvent. This architectural arrangement provides fibrils that maintain high solubility in water and has facilitated the recent exploitation of self‐assembled amphipathic peptide fibrils as functional biomaterials. This article is a critical review of the development and application of self‐assembling amphipathic peptides with a focus on the fundamental insight these types of peptides provide into peptide self‐assembly phenomena. © 2011 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 98: 169–184, 2012.