The Intrinsic Fluorescence of Peptide Self-Assemblies Across pH Levels.

The regulation of solution pH on the structural and optical properties of peptide self-assemblies remains a critical yet unresolved issue in peptide research. This study investigates the heptapeptide Ac-IHIHIQI-NH and its intrinsic fluorescence across a range of pH levels, demonstrating that variations in pH lead to significant changes in the morphology of the self-assembled structures. While the position of the fluorescence emission remains constant-due to the stability provided by the hydrogen bonding network of the peptide backbone-the intensity of the fluorescence exhibits a direct correlation with the degree of self-assembly. This finding underscores a dynamic relationship between structural morphology and optical properties. Notably, the ability of the peptide to self-assemble under diverse pH conditions is a novel observation that contrasts with previously reported literature. By employing a computationally driven approach, complemented by rigorous experimental validation, this work establishes a new paradigm for studying complex interacting systems such as peptide self-assembly. Our findings enhance the understanding of how environmental factors influence peptide behavior and pave the way for the design of innovative peptide-based materials with tunable optical characteristics, with potential applications in bioluminescent probes and diagnostic tools for neurodegenerative diseases.