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.

Amyloid-based nanosensors and nanodevices

“…118,164 Other peptide systems that adopt typical beta-sheet structures have been developed, for example by J. Collier, A. Aggelli, D. Pochan and others, discussed in a recent review. 36 …”

“…In particular, we want to point out that not every reported amphiphilic peptide that forms b-sheets by selfassembly is evidentially an amyloid structure. 35,36 Known amyloid peptide motifs can be combined with lipids, nucleic acids, sugar moieties and other building blocks. In addition, synthetic moieties will expand chemical versatility and functionalization potential.…”

Application and use of differential scanning calorimetry in studies of thermal fluctuation associated with amyloid fibril formation

“…Hydrophobic interactions usually play an important role in thermally induced aggregation of protein molecules, the basic features of which are assumed to be the spatial approach and dehydration of the exposed hydrophobic regions to solvent water (Kauzmann 1959;Tanford 1978;Baldwin 1986;Israelachvili and Wennerström 1996;Chandler 2005). In the amyloid fibrils formed from β 2 -m and Aβ, the hydrophobic and hydrophilic residues may be patterned on the fibril surface (Broome and Hecht 2000;Mandel-Gutfreund and Gregoret 2002;Hecht et al 2004;Saiki et al 2005;Fändrich et al 2009;Bowerman and Nilsson 2012), resulting in transient association upon heating. The dynamic feature of hydration in biomolecular systems causes the remarkably varied entropic and energetic responses of water molecules in the vicinity of hydrophobic, polar, and charged solutes that are frequently reflected in the entropy-enthalpy compensation (Lumry and Rajender 1970;Liu et al 2000).…”

Investigating the Effects of Aromatic Amino Acids on Amphipathic Peptide Self-Assembly and Emergent Hydrogel Viscoelasticity

“…Amphipathic β-sheet peptides composed of alternating hydrophobic and hydrophilic amino acids (with general sequence (XZXZ)n where X is nonpolar and Z is polar) are a privileged class of self-assembling peptide that have been widely used in the design of hydrogel materials [4]. The (FKFE)2 peptide is a prominent member of this class of material that has been frequently studied [5,6].…”