Anthocyanin
degradation from alkaline or heat exposure limits its
practical applications. Peptide-based microencapsulation can enhance
anthocyanin’s physicochemical properties, such as pH and temperature
stability. However, the diversity of amino acids makes investigating
the complex interactions between peptides and anthocyanins experimentally
challenging. In this study, we engineered four amphiphilic α
helix peptides (C6W1, C6W2, C6W4, and C6W6) with varying tryptophan
contents (one, two, four, and six) to explore tryptophan-dependent
interaction mechanisms for improved anthocyanin stability. Molecular
docking and molecular dynamics simulations showed that peptides with
higher tryptophan content exhibit stronger interactions with anthocyanins,
as evidenced by electrostatic forces, Lennard-Jones interactions,
Gibbs free energy, and hydrogen bonds. Notably, the computational
data aligns with our previous experimental findings on the coassembly
and stability enhancement of peptides (C6W1, C6W4) and anthocyanins.
This research offers valuable guidance on peptide design for enhanced
microencapsulation of anthocyanins, potentially improving their physicochemical
properties and broadening their applications.