Self-Assembly of the Tetraphenylethylene-Capped Diserine through a Hierarchical Assembly Process.

We report a new peptide-based urchin-shaped structure prepared through two-step self-assembly of tetraphenylethylene-diserine (TPE-SS). Hydrogelation generated nanobelts through the first stage of self-assembly of TPE-SS; these nanobelts further transformed on silicon wafers into urchin-like microstructures featuring nanosized spines. The presence of the TPE moiety in the hydrogelator resulted in aggregation-induced emission characteristics both in the solution and in the gel phases. TPE-SS has the lowest molecular weight of any TPE-capped hydrogelator with ß-sheet-like structures under physiological pH. This new design strategy appears to be useful for generating three-dimensional self-assembled microstructures and multifunctional biomaterials. We found that TPE-SS is biocompatible with human mesenchymal stem cells and breast cancer cells, making them potential applications in tissue engineering and biomedical research.

Effect of Peptide Sequences on Supramolecular Interactions of Naphthaleneimide/Tripeptide Conjugates.

In this study, we reported a significant difference in the supramolecular hydrogelation of newly discovered NI-GFF (NI-Gly-l-Phe-l-Phe) and NI-FFG (NI-l-Phe-l-Phe-Gly) on the basis of their phase diagrams. With a small difference in the peptide chain between NI-GFF and NI-FFG, we observed a significant difference in their self-assembly properties; NI-GFF formed a stable gel at neutral pH, whereas NI-FFG did not, under the same conditions. From spectroscopic and computational studies, intermolecular π-π interactions and extended hydrogen bonding interactions might reinforce the intermolecular interactions of NI-GFF, which may facilitate the formation of the self-assembled nanostructures and the hydrogel. In addition, the aggregation-induced emission (AIE)-active NI-GFF reveals relatively good biocompatibility compared with that of NI-FFG for two commonly used cell lines, suggesting that it is a promising candidate for use as a supramolecular material in biomedical applications. Our results highlight the importance of tripeptide sequences in a self-assembling hydrogel system.

Fluorescent supramolecular hydrogels self-assembled from tetraphenylethene (TPE)/single amino acid conjugates.

Herein, we report the synthesis of simple TPE/single amino acid conjugates, TPE-Ser and TPE-Asp with side-chains featuring functional groups that may provide an additional hydrogen bonding network for hydrogelation in aqueous medium. TPE-Ser, which has the lowest molecular weight, containing hydroxyl groups undergoes self-assembly into supramolecular hydrogels under physiological pH conditions. TPE-Asp with a carboxylic group side chain undergoes the self-assembly and hydrogelation processes under slightly acidic conditions (pH = 6.0). UV-vis, IR, PL and rheological studies clearly indicate the formation, stability and fluorescence properties of TPE-amino acid hydrogels. TEM micrographs of the hydrogels indicate that the compounds are self-assembled into a nanosheet morphology with random size and shape. Further, in vitro analysis of TPE-Ser and TPE-Asp with 3A6 cells shows that the compounds exhibit unique fluorescence signals in microcellular environments thus making them suitable candidates for bioimaging applications. Overall, these findings highlight the importance of the structure-hydrogelation relationship and provide new insights into the design of single amino-acid-based supramolecular hydrogels.