Spectroscopic Investigation of Hydrogels Formed from Phenylalanine

Supramolecular hydrogels assembled from amino acids, particularly offer promising prospects as biomimetic three-dimensional extracellular matrices. Phenylalanine, an aromatic amino acid, can self-assemble via hydrophobic interactions, notably through 𝜋 - 𝜋 stacking between phenyl rings. Although the self-assembly processes have been studied, the gelation mechanism of phenylalanine as an individual amino acid has received limited attention in the literature. This study focuses on investigating the gelation behavior of phenylalanine. Fluorescence spectroscopy, along with UV- Visible spectroscopy, and Fourier-transform infrared spectroscopy, were employed to elucidate the molecular interactions and the self-assembly process responsible for hydrogel formation. By leveraging fluorescence spectroscopy, this study aims to elucidate the mechanisms underlying the hydrogelation process. The fluorescence properties of the synthesized hydrogels are extensively examined, providing insights into their structural organization and stability, In this study, we employed a simple heating-cooling method for preparing phenylalanine hydrogel resulting in the formation of opaque hydrogels. Spectral analyses revealed the molecular interactions and structural organization, highlighting the relationship between concentration, opacity, and gel properties. Through this study, we investigated the gelation mechanism of a simple molecule using fluorescence spectroscopy, which provides a foundation for exploring the use of the same in other hydrogel-forming systems.