Self-assembled peptide nanostructures for functional materials

Abstract

Nature is an important inspirational source for scientists, and presents complex and elegant examples of adaptive and intelligent systems created by self-assembly. Significant effort has been devoted to understanding these sophisticated systems. The self-assembly process enables us to create supramolecular nanostructures with high order and complexity, and peptide-based self-assembling building blocks can serve as suitable platforms to construct nanostructures showing diverse features and applications. In this review, peptide-based supramolecular assemblies will be discussed in terms of their synthesis, design, characterization and application. Peptide nanostructures are categorized based on their chemical and physical properties and will be examined by rationalizing the influence of peptide design on the resulting morphology and the methods employed to characterize these high order complex systems. Moreover, the application of self-assembled peptide nanomaterials as functional materials in information technologies and environmental sciences will be reviewed by providing examples from recently published high-impact studies.

Peptide‐Thiophene Hybrids as Self‐Assembling Conductive Hydrogels

“…While concerns about amyloidogenic potential of these beta structured peptides need further attention, in vitro and in vivo studies thus far have shown several classes of peptide‐based materials to be biocompatible . Beta‐sheet forming peptides often have the sequence (ZXZX) n , where Z and X represent amino acid residues of alternating hydrophobicity . This alternation results in a peptide amphiphile with distinct faces; the hydrophobic faces tend to interact and sequester the hydrophobic side chains, presenting the hydrophilic residues on the opposite surface for interaction with solvent .…”

“…Beta‐sheet forming peptides often have the sequence (ZXZX) n , where Z and X represent amino acid residues of alternating hydrophobicity . This alternation results in a peptide amphiphile with distinct faces; the hydrophobic faces tend to interact and sequester the hydrophobic side chains, presenting the hydrophilic residues on the opposite surface for interaction with solvent . The exposed hydrophilic face offers opportunity to initiate assembly with pH changes, increasing the likelihood of creating a peptide hydrogel.…”

“…[6,7] Beta-sheet forming peptides often have the sequence (ZXZX) n , where Z and X represent amino acid residues of alternating hydrophobicity. [23] This alternation results in a peptide amphiphile with distinct faces; the hydrophobic faces tend to interact and sequester the hydrophobic side chains, presenting…”

Selective detection of α4β1 integrin (VLA‐4)‐expressing cells using peptide‐functionalized nanostructured materials mimicking endothelial surfaces adjacent to inflammatory sites

“…In recent years, bioactive synthetic surfaces formed by self‐assembled monolayers (SAMs) of functionalized nanoparticles have been frequently used in cell biology due to their small scale, unique physical properties, and multiple surface functionalization . Compared to the SAMs of simple bioactive molecules, SAMs of biofunctionalized nanoparticles have advantages due to the fact that these SAMs provide a large surface area that allows a multiplicity of contact points between the cells and the nanomaterials, resulting in a more efficient information transfer and multifunctionalities implemented in the same particle, in the nanoscale …”

Three‐Dimensional Laminin Mimetic Peptide Nanofiber Gels for In Vitro Neural Differentiation

“…Self-assembling peptide amphiphile nanofiber gels have been widely used in 2D and 3D cellular culture studies [13] and are promising candidates for regenerative medicine applications due to their biocompatibility, biodegradability, and incorporation of bioactive signals. [14,15] Peptide amphiphile systems have been extensively used in neural regeneration applications, and bioactive epitopes derived from ECM proteins, such as the laminin-derived IKVAV and YIGSR, fibronectin-derived RGD, and tenascin-C-derived VFDNFVLK sequences, have been shown to induce neural differentiation, attachment, and migration. [16][17][18][19] The imitation of ECM proteins is especially important in this context, as integrin receptors and similar mechanotransduction elements are essential for cellular adhesion, homing, and differentiation.…”