Casein phosphopeptide interferes the interactions between ferritin and ion irons.

ABSTRACT

Ferritin, a vital protein required to store iron in a cage-like structure, is critical for maintaining iron balance. Ferritin can be attacked by free radicals during iron reduction and release, thereby leading to oxidative damage. Whether other biomacromolecules such as casein phosphopeptides (CPP) could influence the ferritin's function in iron oxidation and release and affect the ferritin stability remains unclear. This study aims to investigate the effect of CPP on the ferritin­iron ion interaction, thereby focusing on role of CPP on ferritin stability. Results showed that CPP weakened the iron oxidation activity of ferritin but promoted iron release. Moreover, CPP could effectively chelate iron, capture hydroxyl radicals, and reduce the degradation of ferritin. This study highlights the role of CPP in the ferritin­iron relationship, and lays a foundation for understanding the interaction between ferritin, peptides, and metal ions.