Self-assembly of amphipathic β-sheet peptides: insights and applications

• Published in: Biopolymers Vol. 98; no. 3; pp. 169 - 184
• Main Authors: Bowerman, Charles J, Nilsson, Bradley L
• Format: Journal Article
• Language: English
• Published: United States 2012
• Subjects: Amino Acid Sequence; Hydrogels; Microscopy, Electron, Transmission; Models, Molecular; Molecular Sequence Data; Peptides - chemistry; Protein Structure, Secondary; Solubility; Water
• ISSN: 0006-3525
• DOI: 10.1002/bip.22058

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.