Short peptide hydrogels are attractive biomaterials but typically suffer from limited mechanical properties. Inclusion of other nanomaterials can serve the dual purpose of hydrogel reinforcement and of conferring additional physicochemical properties ( e. g., self-healing, conductivity), as long as they do not hamper peptide self-assembly. In particular, nanocarbons are ideal candidates, and their physicochemical properties have demonstrated great potential in nanocarbon-polymer gel biomaterials for tissue engineering or drug delivery. Recently, increasing interest in supramolecular hydrogels drove research also on their enhancement with nanocarbons. However, little is known on the effect of nanocarbon morphology on the self-assembly of short peptides, which are among the most popular hydrogel building blocks. In this work, three different oxidized nanocarbons ( i. e., carbon nanotube or CNT as 1D material, graphene oxide sheet or GO as 2D material, and carbon nanohorn or CNH as 3D material) were evaluated for their effects on the self-assembly of the unprotected tripeptide Leu-Phe-Phe at physiological conditions. Supramolecular hydrogels were obtained in all cases, and viscoelastic properties were clearly affected by the nanocarbons, which increased stiffness and resistance to applied stress. Notably, self-healing behavior was observed only in the case of CNTs. Tripeptide-nanotube interaction was noted already in solution prior to self-assembly, with the tripeptide acting as a dispersing agent in phosphate buffer. Experimental and in silico investigation of the interaction between peptide and CNTs suggests that the latter acts as nucleation templates for self-assembly and reassembly. Overall, we provide useful insights for the future design of composite biomaterials with acquired properties.

We report the first histidine-containing self-assembling tripeptide devoid of capping groups that forms a thermoreversible hydrogel under physiological conditions and catalyses hydrolysis of an ester, providing a minimalist building block for functional soft materials.

Dipeptides and their cyclized 2,5-piperazinedione (or diketopiperazine, DKP) derivatives are attractive building blocks for supra­molecular hydrogels. The Phe-Phe, (p-nitro)-Phe-Phe, and Phe-Val dipeptides and their corresponding DKPs are studied for self-assembly in water. The DKPs were obtained in high yields by microwave-assisted cyclization­ of the dipeptides in water, demonstrating that use of their methyl ester derivatives as reported in the literature is not necessary for successful cyclization. Single-crystal XRD structures are reported for two DKPs as well as stable hydrogels at neutral pH.

N-(4-Nitrobenzoyl)-Phe self-assembled into at ransparent supramolecular hydrogel, whichd isplayed high fibroblast and keratinocyte cell viability.T he compound showed am ild antimicrobial activity against E. coli both as ah ydrogel and in solution.S ingle-crystal XRD data revealed packing details,i ncluding protonation of the C-terminus due to an apparent pK a shift, as confirmed by pH titrations. MicroRaman analysisr evealed almosti denticalf eaturesb etween the gel and crystal states,a lthough more disorder in the former. The hydrogel is thermoreversible and disassemblesw ithin a range of temperaturest hat can be fine-tunedb ye xperimental conditions, such as gelator concentration. At the minimum gellingc oncentration of 0.63 wt %, the hydrogel disassembles in ap hysiological temperature range of 39-42 8C, thus opening the way to its potential use as ab iomaterial.[a] Dr.Supporting information and the ORCID identification number(s) for the author(s) of this articlecan be found under: https://doi.

Supramolecular hydrogels offer interesting opportunities for co-assembly with drugs towards sustained release over time, which could be achieved given that the drug participates in the hydrogel nanostructure, and it is not simply physically entrapped within the gel matrix. D Leu-Phe-Phe is an attractive building block of biomaterials in light of the peptide's inherent biocompatibility and biodegradability. This study evaluates the assembly of the tripeptide in the presence of either of the anti-inflammatory drugs ketoprofen or naproxen at levels analogous to commercial gel formulations. Fourier-transformed infrared (FT-IR), circular dichroism, Thioflavin T fluorescence, transmission electron microscopy (TEM), and oscillatory rheometry are used. Drug release over time is monitored by means of reverse-phase high performance liquid chromatography, and shows different kinetics for the two drugs.