Fluorescence Studies of Amino Acid and Peptide‐Based Hydrogels: Unveiling Self‐Assembly and Structural Insights

Abstract Fluorescence spectroscopy has emerged as a powerful tool for studying the self‐assembly, structural integrity, and dynamic behaviors of amino acid and peptide‐based hydrogels. Unlike fluorescence microscopy, which visualizes spatial distributions, fluorescence spectroscopy delves into the molecular interactions and environmental changes within these hydrogels. This review highlights the intrinsic fluorescence of amino acids such as tryptophan, tyrosine, and phenylalanine, alongside modifications such as Fmoc groups and the use of external probes, to elucidate gelation mechanisms and aggregation dynamics. Key phenomena such as aggregation‐induced emission (AIE), aggregation‐induced quenching (AIQ), time‐resolved fluorescence, and fluorescence resonance energy transfer (FRET) techniques provide insights into favorable and unfavorable assembly processes. The ability of fluorescence spectroscopy to monitor hydrogels in their native wet state without structural disruptions caused by drying presents a significant advantage over traditional morphological techniques such as TEM and SEM. This review underscores the importance of fluorescence spectroscopy in advancing the design and application of amino acid and peptide‐based hydrogels, with potential implications for biomaterials, drug delivery, and biosensing. The integration of fluorescence spectroscopy with complementary techniques holds great promise for unlocking new possibilities in hydrogel research.