Self-assembly non-covalent binding mechanism of lycopene-protein-chondroitin sulfate ternary nanoparticles: Multidimensional characterization and molecular dynamics simulation.
TL;DR
How protein structural differences regulate the performance of protein-polysaccharide nanoparticles is revealed and theoretical and technical insights into the precise design and practical application of delivery systems for LYC and other lipophilic bioactive compounds are provided.
Abstract
To overcome lycopene's (LYC's) poor water solubility, oxidative instability, and low bioaccessibility, chondroitin sulfate (CS) was used as a stabilizing layer to construct LYC-Protein-CS nanoparticles (LYC-Protein-CS NPs) using different proteins. Their structures and delivery performance were compared to clarify how protein structure influences the delivery of lipophilic bioactives. Zein's layered folding and hydrophobic-hydrophilic partitioning promoted assembly with CS, forming a compact core-shell network. Consequently, LYC-Zein-CS showed superior encapsulation, dispersion stability, antioxidant activity, and gastrointestinal release behavior. Compared with free LYC, this system increased apparent bioaccessibility by 12.95-fold in the gastric phase and 14.87-fold in the intestinal phase during simulated digestion. These findings reveal how protein structural differences regulate the performance of protein-polysaccharide nanoparticles and provide theoretical and technical insights into the precise design and practical application of delivery systems for LYC and other lipophilic bioactive compounds.
