Ovalbumin-derived peptide, VLVNAIVFKGL, demonstrated self-assembling and gelation properties. However, the extent of self-assembly via solvent-switching and the bioactive potential of the ordered peptide aggregates is unknown. In silico analysis using AGGRESCAN, TANGO, ANuPP, and GAP predicted a high propensity to self-assemble into amyloid-like aggregates. Thioflavin T fluorescence assay confirmed enhanced self-assembly at low solvent concentrations (0.03-5% DMSO) and increasing peptide concentration (4-400 μM). Transmission electron microscopy showed enhanced formation of interconnected fibrillar networks at 400 μM. Mechanical properties assessed via rheology confirmed the hydrogelation of the fibrillar networks with high fibrillar stability in simulated gastrointestinal fluids. Oxidative stress assays using showed a 21.48 ± 3.37% reduction in juglone-induced reactive oxygen species production by the hydrogel. In silico analysis further predicted the cell-penetrating and nontoxic characteristics of the peptide, highlighting the potential biocompatibility. Taken together, these findings support the development of VLVNAIVFKGL as an antioxidant peptide hydrogel for edible applications.
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