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Updated: Sep 7, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Self-assembly non-covalent binding mechanism of lycopene-protein-chondroitin sulfate ternary nanoparticles:
Weiyu Yan1, Qian Cui1, Tian Qiu1
1Tianjin International Cooperation Research Centre of Food Nutrition/Safety and Medicinal Chemistry, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China.
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.
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