Self-Assembled Peptide Nanostructures for ECM Biomimicry

Abstract

Proteins are functional building blocks of living organisms that exert a wide variety of functions, but their synthesis and industrial production can be cumbersome and expensive. By contrast, short peptides are very convenient to prepare at a low cost on a large scale, and their self-assembly into nanostructures and gels is a popular avenue for protein biomimicry. In this Review, we will analyze the last 5-year progress on the incorporation of bioactive motifs into self-assembling peptides to mimic functional proteins of the extracellular matrix (ECM) and guide cell fate inside hydrogel scaffolds.

Development of Two-Layer Hybrid Scaffolds Based on Oxidized Polyvinyl Alcohol and Bioactivated Chitosan Sponges for Tissue Engineering Purposes

“…The SAPs are protein fragments that in solution self-organize in very stable amphiphilic-beta sheets conformation by hydrogen bonds; thus, they have great potential in tissue engineering, including peripheral nerve regeneration [ 20 , 40 , 41 ] due to a 3D self-arrangement mimicking ECM ultrastructural organization [ 41 , 42 ]. Furthermore, they also display high stability against thermal, chemical, and proteolytic attacks [ 43 ].…”

Cyclodipeptides: From Their Green Synthesis to Anti-Age Activity

“…Future studies may be directed towards the development of suitable formulations to maximize their ability to be enriched in the dermis for cosmetic use, or elsewhere for systemic effects, given the established health benefits from DKP5 administration. For instance, combination with linear short peptides that can self-assemble into nanostructured hydrogels and mimic natural components of the extracellular matrix [ 65 ] could offer a promising avenue for cosmetic formulations. The mechanistic elucidation of the observed effects in terms of cell protection from UV damage certainly deserves further investigation to better understand how these biomolecules exert their bioactivity, so that their use can be extended beyond cosmetics, to the preservation of human health.…”

Cell Adhesion Motif-Functionalized Lipopeptides: Nanostructure and Selective Myoblast Cytocompatibility

“…The integrin cell adhesion peptides RGD and RGDS are minimal units of a domain present in proteins such as fibrinogen, fibronectin, and vitronectin. 1 , 2 These sequences have been extensively used in the development of synthetic bionanomaterials for applications in cell growth and differentiation or tissue scaffolding 3 − 12 and for the delivery of therapeutics. 13 − 15 The RGDS tetrapeptide has antithrombolytic activity resulting from the inhibition of platelet aggregation due to the fibrinogen recognition sequence.…”

“…The integrin cell adhesion peptides RGD and RGDS are minimal units of a domain present in proteins such as fibrinogen, fibronectin, and vitronectin. , These sequences have been extensively used in the development of synthetic bionanomaterials for applications in cell growth and differentiation or tissue scaffolding − and for the delivery of therapeutics. − The RGDS tetrapeptide has antithrombolytic activity resulting from the inhibition of platelet aggregation due to the fibrinogen recognition sequence. , The RGD and RGDS motifs have been incorporated into lipopeptides, one type of peptide amphiphile (PA). ,,− In some reports, the RGDS tetrapeptide is purported to have enhanced bioactivity compared to RGD due to the additional serine residue. − The self-assembly of materials containing RGD-peptide sequences has been reviewed elsewhere. , …”