Influence of self-assembly on the reactive sulfhydryl and antioxidant activity of aggregation-prone ovalbumin-derived peptides

Ovalbumin-derived peptides IFYCPIAIM, NIFYCPIAIM and YCPIAIMSA, containing a common region YCPIAIM, were previously identified as aggregation-prone with variable fibril formation. In this study, we elucidated self-assembly mechanisms of the peptides, by determining influence on sulfhydryl group accessibility. The free content antioxidant capacity results demonstrate that assemble into β-sheets, possibly involving hydrogen bonding groups. NIFYCPIAIM, IFYCPIAIM in decreasing order, had largest particle size, thioflavin T fluorescence, reactive content, activities. This demonstrates which is influenced cysteine residue position relative to N-terminal peptide, dependent fibrillation. Rheological studies further demonstrated non-Newtonian shear-thinning behavior peptides. provide valuable insight peptide self-assembly, imperative for future design bioactive hydrogels promising biomechanical properties biomaterial applications.