Engineering Biocompatible Scaffolds through the Design of Elastin‐Based Short Peptides

Abstract

A small library of short peptides has been synthesized based upon the repeat tetrapeptide sequence Gly‐Val‐Ala‐Pro (GVAP) which is found in the hydrophobic domain of tropoelastin. Of the five peptides synthesized, four formed self‐supporting hydrogels with similar secondary structures. The ability to tune the mechanical properties of the resultant hydrogels was demonstrated, and this is understood in relation to fiber bundling. Finally, the cytotoxicity of these elastin‐based short peptide hydrogels towards HeLa cells was assessed, with clear evidence that increased aromaticity of the peptide is detrimental towards cell viability.

Self-Assembly of Stable Nanoscale Platelets from Designed Elastin-like Peptide–Collagen-like Peptide Bioconjugates

“…Similar to the behavior of thermoresponsive synthetic polymers, a characteristic property of ELPs is their lower critical solution temperature (LCST)-like behavior (also termed an inverse transition temperature), which endows ELPs with the ability to be used as building blocks for the assembly of nanostructures. − A wide variety of studies have demonstrated the versatility of ELP design and resulting transition temperature ,, and the application of these principles to the production of hydrogel matrices and drug delivery vehicles. − While these studies illustrate the versatility of the ELPs as self-assembling building blocks, essentially all of the ELPs employed are recombinamers with tens or even hundreds of pentapeptide repeats. Short synthetic ELPs (peptides) on their own have been rarely used as bulk materials for biomedical applications, possibly due to their relatively high transition temperature, , although recent studies suggest the utility of the conjugation of short ELPs to polymers and dendrimers to control LCST-like behavior and self-assembly − as well as the impact of protecting groups on the thermally induced transitions of short ELPs …”

“…Short synthetic ELPs (peptides) on their own have been rarely used as bulk materials for biomedical applications, possibly due to their relatively high transition temperature, 38,39 although recent studies suggest the utility of the conjugation of short ELPs to polymers and dendrimers to control LCST-like behavior and self-assembly 45−49 as well as the impact of protecting groups on the thermally induced transitions of short ELPs. 50 In our previous work, we demonstrated that this limitation can be easily overcome by simply conjugating short ELPs with a triple-helix-forming CLP. 51 The resulting ELP−CLP bioconjugate exhibited a remarkable reduction in the inverse transition temperature (T t ) of the ELP domain upon formation of the CLP triple helix, so that nanostructures can be formed under aqueous conditions in a temperature range of relevance for biomaterials applications.…”

Scaffolds Formed via the Non-Equilibrium Supramolecular Assembly of the Synergistic ECM Peptides RGD and PHSRN Demonstrate Improved Cell Attachment in 3D

“…The self-assembly of biomolecules have received significant attention as a facile route to fabricate bioinspired scaffolds with porous, three-dimensional (3D) architectures, that have increasingly well-understood mechanisms to control their formation [1,2,3]. Nevertheless, for effective cell culture and tissue growth, significant functionalization is required to truly exploit their promise as biomaterials; the engineering of biomaterial scaffolds should to not only mechanically support cells, but also actively modulate cellular activities [4,5,6].…”

Structural Characterization of a New Collagen Biomimetic Octapeptide with Nanoscale Self‐Assembly Potential: Experimental and Theoretical Approaches

“…Among these peptides, Fmoc-FGVAPF shows a lateral aggregation phenomenon. [28] The sequence APF is also present in collagen and could be a key motif in its hierarchical organization.…”