Disulfide crosslinking and helical coiling of peptide micelles facilitate the formation of a printable hydrogel

Abstract

Tripeptides self-assembled into aligned micelles which transformed into nanohelices via covalent and noncovalent interactions to give a printable hydrogel.

Short Peptide-Based Smart Thixotropic Hydrogels

“…Next, Qi and Wang et al fabricated a tripeptide in which the N-terminal of the peptide was capped with an Fmoc group. The central part is composed of a well-known self-assembling PhePhe motif, and Cys at the C-terminal for the crosslinking of the sulfhydryl group undergoes self-assembly in 0.5 M NaOH solution to form a stable, self-supporting hydrogel with a helical network ( Figure 9 F, Table 4 ) [ 114 ]. The thixotropic behavior of the hydrogel was evaluated with the help of a time-dependent step-strain experiment in which alternation of low (γ = 1.0%) and high (γ = 100%) strain was applied to check gel-sol-gel transitions ( Figure 9 G).…”

“…( G )Thixotropic analysis and injectability of the hydrogelator T 3 P5; reproduced with permission from Ref. [ 114 ]. Copyright (2019) The Royal Society of Chemistry.…”

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

“…Furthermore, the work on selected Ac-Phe-X-Asp-NH 2 sequence with high aspect ratio; Ac-Phe-Ile-Asp-NH 2 , suggested the requirement of the non-aromatic and uncharged residue in this tripeptide, which in this case was isoleucine-to be at least hydrophobic as well to facilitated high aspect-ratio nanostructure and aid hydrogel formation (Sahoo et al, 2018a). The study by Yang et al, on structural transition in Fmoc-Phe-Phe-Cys-OH from parallel-aligned worm-like micelles to entangled, coiled micelles persuaded by the cross-linking of the disulfide bonding, elucidated the relationship between micelle chirality and gel properties and suggested a strategy to fabricate materials with controlled chirality by means of synchronized non-covalent and covalent self-assembly (Yang et al, 2019). A series of Fmoc-protected tripeptide containing β-amino acid from H-βAla-His-OH [L-carnosine (Car)] joined by covalent link to different Fmoc-L-amino acids with a wide range of sidechains having different hydrophobicities were observed by Das et al The tripeptides were found to be proteolytically stable under physiological condition and produce helical structures and the gelation capability to depend on the hydrophobicity of the side chain moiety where the additional π-π stacking interaction by the phenyl group supported the process.…”

Peptide-Based Hydrogels: New Materials for Biosensing and Biomedical Applications

“…An arginine-glycine-aspartate peptide hydrogel improved the adhesion and growth of stem cells, and the in vivo results showed the formation of more blood vessels inside the hydrogel compared to other systems, demonstrating a high potential of such hydrogel systems for tissue engineering applications. Yang et al reported that the Fmoc-protected phenylalanine-phenylalanine-cysteine could self-assemble into micelles at high pH values, followed by a spontaneous transformation into a stable hydrogel [ 31 ]. Mahapatra et al prepared a series of pH-sensitive Fmoc-modified tripeptide hydrogels containing β -amino acid showing thermoreversibility and proteolytic stability (against proteinase K enzyme) [ 32 ].…”