We have discovered a unique series of tripeptides that form strong hydrogels. Previous studies found that the tripeptide Glycine-Histidine-Glycine forms a hydrogel at low concentration and neutral pH. The peptide aggregates into oligomers which ultimately form a gel network of micron-size, crystalline fibrils that are highly entangled and volume spanning. These hydrogels have shown potential in biomedical applications such as drug-delivery and cell scaffolds with the advantage of low-cost and biocompatibility. This study seeks to understand the solubility conditions that favor the fibril phase and to investigate the mechanical properties of the gel using rheology. We explored the tunability of the material for future developments by screening formation conditions. We show that the gel strength, microstructure, and formation kinetics can be tuned by adjusting the pH and peptide concentration. We aim with this work to improve aggregation models and develop this novel material for biomedical applications.

Self-assembly of glycine-histidine-glycine hydrogels

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.