Nanoscale Characterization of Self-Assembled Supramolecular Hydrogel

Molecular self-assembly is a process of key importance in natural systems, nanotechnology and fabrication of advanced materials. The study of short peptide and amino acid self-assembly provides a fascinating and diverse building block repertoire for nanotechnological applications due to unique structure, relative facile synthesis, and biocompatibility.

Short peptides and amino acids can form three-dimensional (3D) hydrogels that can support the growth of living cells. These materials are being used for biomedical applications such as tissue regeneration. There is growing interest in harnesing minimal self-assembling peptides and amino acids as hydrogel networks that support cell growth. Yet, significant questions persist concerning the mechanism of self-assembly and the relationship between the molecular structure of the assembled materials, their emergent viscoelastic and mehanical properties.

In previous work, we demonstrated the synergistic effect of the co-assembly of two ultra-short peptide on the mechanical propeties of the resulting hybrid hydrogel. Here, we present the systamatic exploration of the effect of different environmental conditions on the self-assembly process. We investigated various solvent compositions and peptide concentrations, using microscopic analysis and X-ray powder diffraction, demonstrating the diversity of the structures morphologies. Finally, we generated a phase diagram for the assemblies.

This work contributes to a better understanding and characterization of the self-assembling peptides and functionalized amino acids in order to rationally design hydrogels with desired properties. We focus on the challenges of understanding the structure-function relationship of these materials, leading to future applications in biomedical and material science.