Biomimetic peptide self-assembly for functional materials

Abstract

Biomolecular systems have evolved to form a rich variety of supramolecular materials and machinery fundamental to cellular function. The assembly of these structures commonly involves interactions between specific molecular building blocks, a strategy that can also be replicated in an artificial setting to prepare functional materials. The selfassembly of synthetic biomimetic peptides allows us to explore chemical and sequence space beyond that used routinely by biology. In this Review, we discuss recent conceptual and experimental advances in self-assembly of artificial peptidic materials. In particular, we explore how naturally-occurring structures and phenomena have inspired the development of functional biomimetic materials that we can harness for potential interactions with biological systems. As our fundamental understanding of peptide self-assembly evolves, increasingly sophisticated materials and applications emerge and lead to the development of a new set of building blocks and assembly principles relevant to materials science, molecular biology, nanotechnology and precision medicine.

A Global Review on Short Peptides: Frontiers and Perspectives

“…Nanoparticles’ conjungtion with inter alia tumor-homing peptides is an attractive avenue for tumor-targeted therapy [ 136 , 137 ]. The advances in the synthesis of supra-molecular assemblies prompt the development of theranostics (which possess specific smart features, such as programmability, multifunctionality, sensitivity, precise selectivity, biosafety) and are promising agents for personalized, smart medicine [ 126 , 138 , 139 ].…”

“…As an example, short peptide-based inhibitors of amyloid β aggregation in Alzheimer’s disease with reduced cytotoxicity are good drug candidates [ 32 , 33 ]. Notably, very short peptides, like diphenylalanine and related compounds such as tert -butoxycarbonyl derivative ( Table 2 [ 126 ]), are the core recognition motifs of β-amyloid polypeptides [ 98 , 126 ]. Fibrillar dynamic self-assembly behaviour of short peptides, leading to amyloid-like supramolecular structures, is a key insight into the nucleation, oligomerization, and the physical properties of amyloid fibrils [ 126 ].…”

“…Theses very short peptides as well as cell-penetrating peptides are of relevance to the highly efficient drug delivery systems (to target cells and subcellular organelles) and the prevention of amyloid β aggreagation [ 316 ]. Interesting and promising aspects of delivery strategy are peptide-based gel matrices to drug encapsulation [ 126 ]. Peptide-based therapeutic drugs induce the neuronal growth, modulate neurogenesis [ 317 ], and finally improve spatial memory.…”

Peptide-Based Nanomaterials for Tumor Immunotherapy

“…Like the phenomenon of protein self-assembly that exists widely in nature, peptides can also self-assemble by using hydrogen bonding, electrostatic interaction, hydrophobic interaction, and π–π stacking between peptide bonds and amino acid residues, which is orderly, controllable, and stable [ 33 ]. Peptide self-assembly is generally based on their secondary structure or hydrophobicity.…”

Heterotypic Supramolecular Hydrogels Formed by Noncovalent Interactions in Inflammasomes

“…Peptides, as the building blocks for supramolecular assemblies, have received considerable research attention [ 1 , 2 , 3 , 4 , 5 , 6 , 7 ] because peptides are biodegradable and easily accessible. Generally, when the concentration of a self-assembling peptide reaches a certain threshold, intermolecular noncovalent interactions would result in a network of peptide nanofibers, which are able to hold water in the interstitial spaces to form hydrogels [ 8 , 9 ].…”