Self-assemble peptide biomaterials and their biomedical applications

Abstract

Inspired by self-assembling peptides found in native proteins, deliberately designed engineered peptides have shown outstanding biocompatibility, biodegradability, and extracellular matrix-mimicking microenvironments. Assembly of the peptides can be triggered by external stimuli, such as electrolytes, temperature, and pH. The formation of nanostructures and subsequent nanocomposite materials often occur under physiological conditions. The respective properties of side chains in each amino acids provide numerous sites for chemical modification and conjugation choices of the peptides, enabling various resulting supramolecular nanostructures and hydrogels with adjustable mechanical and physicochemical properties. Moreover, additional functionalities can be easily induced into the hydrogels, including shear-thinning, bioactivity, self-healing, and shape memory. It further broaden the scope of application of self-assemble peptide materials. This review outlines designs of self-assembly peptide (β-sheet, α-helix, collagen-like peptides, elastin-like polypeptides, and peptide amphiphiles) with potential additional functionalities and their biomedical applications in bioprinting, tissue engineering, and drug delivery.

Materials promoting viral gene delivery

“…The intrinsic ability of some peptides to selfassemble into higher order structures allow for numerous applications as functional biomaterials. 330,331 In the last ten years, peptide fibrils caused a paradigm shift in viral gene delivery from using mostly spherical particles to anisotropic, fibrillar nanocarriers, due to their convenient handling and high TE.…”

<p>Delivery of MSCs with a Hybrid β-Sheet Peptide Hydrogel Consisting IGF-1C Domain and D-Form Peptide for Acute Kidney Injury Therapy</p>

“…[1][2][3] Self-assembling peptides, which self-organize from naturally building blocks into supramolecular nanofibrous structures, can be used to recreate native stem cell microenvironments in vivo. 4,5 The initial and rational design for self-assembling peptides was inspired by β-sheet and α-helical structures found in naturally occurring proteins. 2,4,6,7 Insights into peptide folding and intramolecular interactions that drive self-assembly have led to the emergence of customized de novo motifs.…”

Ultrashort Peptide Self-Assembly: Front-Runners to Transport Drug and Gene Cargos

“…π-π stacking between large π-conjugated surfaces provides an overall stability to supramolecular polymers bound together by non-covalent interactions (Cockroft et al, 2005). Various collagen like peptides mimic the fibril formation and assemble into higher order hierarchical structures through π-π stacking interactions (Chen and Zou, 2019). The hypothesis put forward by Gazit et al regarding the lead role played by aromatic interactions in the self-assembly of peptide nanotubes/amyloidlike structures has been established time and again (Reches and Gazit, 2005).…”

“…(Kumar et al, 2015;Li I.C. et al, 2016;Moore and Hartgerink, 2017;Lopez-Silva et al, 2018;Chen and Zou, 2019) In a two-component system, in which a porphyrin cap is combined with a cyclic peptide the combination of various binding forces, e.g., hydrogen bonding, metal coordination, and dynamic covalent bonds, allows the delivery of encapsulated ligand (Ozores et al, 2017). These supramolecular injectable biomaterials, that can mimic the natural extracellular matrix nanostructure and show marked cellular infiltration, are ideal scaffolds for tissue engineering strategies.…”