Bio-Inspired Casein-Derived Antioxidant Peptides Exhibiting a Dual Direct/Indirect Mode of Action.
Gizella CsireFrançois DupireLaetitia Canabady-RochelleKatalin SelmecziLoic StefanPublished in: Inorganic chemistry (2022)
Antioxidant compounds are chemicals of primary importance, especially for their applications in nutrition and healthcare, thanks to their abilities to prevent oxidation processes and to limit and/or rebalance the oxidative stress, well-known for its impact on a wide variety of diseases. While several biomolecules are well-known for their antioxidant properties ( e.g. , ascorbic acid, carotenoids, phenolic derivatives), bio-sourced antioxidants have drawn considerable attention in the last decades, especially bioactive peptides, mainly obtained by the hydrolysis process. Antioxidant peptide sequences are mainly identified a posteriori, thanks to fastidious and time-consuming approaches and techniques, limiting the discovery of new efficient peptides. In this context and taking inspiration from nature, we report herein on a new series of three bio-inspired antioxidant peptides derived from the milk protein casein. These phosphopeptides, designed to chelate the redox-active iron(III) and forming highly soluble complexes up to pH 9, act both as indirect ( i.e ., inhibition of the metal redox activity) and direct ( i.e ., radical scavenging) antioxidants.