Multicomponent peptide assemblies

Abstract

Self-assembled peptide nanostructures have been increasingly exploited as functional materials for applications in biomedicine and energy. The emergent properties of these nanomaterials determine the applications for which they can be exploited. It has recently been appreciated that nanomaterials composed of multicomponent coassembled peptides often display unique emergent properties that have the potential to dramatically expand the functional utility of peptide-based materials. This review presents recent efforts in the development of multicomponent peptide assemblies. The discussion includes multicomponent assemblies derived from short low molecular weight peptides, peptide amphiphiles, coiled coil peptides, collagen, and β-sheet peptides. The design, structure, emergent properties, and applications for these multicomponent assemblies are presented in order to illustrate the potential of these formulations as sophisticated next-generation bio-inspired materials.

Self‐assembly of a Sequence‐shuffled Short Peptide Amphiphile Triggered by Metal Ions into Terraced Nanodome‐like Structures

“…The advances in peptide‐based nanotechnology and its application in material science, is receiving tremendous attention due to extraordinary and high potential self‐assembling behaviour and therefore are highly demanded in nanotechnology . Exploitation of significant short peptide conjugates may have great potential to produce highly ordered assemblies with defined topologies, but the precise control still a challenging task to direct the peptide self organisation into desired functionality.…”

Tyrosine‐Rich Peptides as a Platform for Assembly and Material Synthesis

“…[5,84,85] The design principles rely mainly on controlling the amphiphilicity, sequence periodicity, aromatic interaction, and charge distribution in the assembling units. In this regard, the advantageous features of peptide assembly are becoming more prominent in that the desired bulk properties of the resultant materials can be intricately adjusted by controlling the individual building blocks.…”

Peptide Nanomaterials Designed from Natural Supramolecular Systems

“…Nanofiber structures are widely observed in natural systems, such as silk, collagen, amyloid, viruses, and cytoskeleton. For instance, natural amyloid proteins such as amyloid‐β peptide (Aβ) and tau protein form similar fibrous assemblies that consist of β‐sheet‐rich sequences . Inspired by the natural fibers that are formed by the self‐assembly of building block units, artificial peptide nanofibers have been developed for various applications in the fields of biomedicine, tissue engineering, renewable energy, environmental science, nanotechnology, and material science ,,,.…”

“…Advantages of the peptide‐based nanofibers compared with other polymeric nanofibers include that (1) the nanofiber‐forming peptide units are known and can be chemically tuned, and (2) stimulus‐responsive groups can be introduced to the peptide moiety to control the structures of the nanofibers. The peptide nanofibers can be categorized into several groups, such as amyloid‐like structures, β‐sheet peptides with alternating hydrophilic and hydrophobic amino acids, peptide‐synthetic hybrids including peptide amphiphiles, and β‐helical coiled‐coil motifs ,,…”

“…In pioneering work by Zhang et al., peptides of alternating hydrophilic and hydrophobic amino acid residues, Ac−(AEAEAKAK) 2 −NH 2 (EAK16), which was originally found in a yeast protein zuotin, were self‐assembled to form a hydrogel . Similar types of amphipathic peptides such as Ac−(FKFE) 2 −NH 2 , Ac−(RADA) 4 −NH 2 , and QQKFQFQFEQQ (Q11) have been designed to form self‐assembled nanofibers . Based on the amphipathic peptides, we developed a C 3 ‐symmetric “Wheel‐FKFE” consisting of three FKFECKFE peptides connected to the arm of the C 3 ‐symmetric core at the cysteine residue placed at the middle of the sequence, whose core and peptides can be considered to act as a hub and spokes of a wheel, respectively (Figure a) .…”