Physicochemical stability-increasing effects of anthocyanin via a co-assembly approach with an amphiphilic peptide.

To enhance the stability of anthocyanin, an amphiphilic peptide C6 with tryptophan amino acid was used to co-assemble with anthocyanin C3G. The characterization, stabilities, and antioxidant activity of peptide-anthocyanin (C6-C3G) nanocomposites (70.82 ± 12.41 nm) were investigated. To illustrate the interaction between peptide and anthocyanin, circular dichroism spectroscopy and fluorescence quenching method were used. Here, the peptide C6 switches from random coil structure to β-sheet structure and the fluorescence of tryptophan amino acid in peptide quenched during the intermolecular interaction between them, which was further confirmed a static quenching. The nanocomposites significantly enhance the stabilities of anthocyanin to different alkaline conditions, high temperature of 80 °C, long time storage, and various concentration of Cu ion. In addition, it maintained the excellent intrinsic capacity of anthocyanin to scavenge free radicals. The approach of using an amphiphilic peptide to enhance the stabilities of anthocyanin presents a high potential to expand its application.