ArticleFoods (Basel, Switzerland)2023
The Mechanism Underlying the Amylose-Zein Complexation Process and the Stability of the Molecular Conformation of Amylose-Zein Complexes in Water Based on Molecular Dynamics Simulation.
Article in Foods (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Modification of coconut 11S globulin by coffee phenolic acids: Molecular mechanisms governing enhanced digestibility and antioxidant activity.Food chemistry: X · 2025Article
- Sustainable Hybrid Latexes Derived from Starch Bioparticles and Biobased Monomers.Biomacromolecules · 2025Article
- Synergistic Interactions of Oxidized Amylose Silver Nanoparticles and Topically Applicable Antibiotics Against Staphylococcus aureus.Current microbiology · 2025Article
- Evaluation of amylose content: Structural and functional properties, analytical techniques, and future prospects.Food chemistry: X · 2024Review
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7 authors.
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Abstract
The aim of this study was to employ molecular dynamics simulations to elucidate the mechanism involved in amylose-zein complexation and the stability of the molecular conformation of amylose-zein complexes in water at the atomic and molecular levels. The average root mean square deviation and radius of gyration were lower for amylose-zein complexes (1.11 nm and 1 nm, respectively) than for amylose (2.13 nm and 1.2 nm, respectively), suggesting a significantly higher conformational stability for amylose-zein complexes than for amylose in water. The results of radial distribution function, solvent-accessible surface area, and intramolecular and intermolecular hydrogen bonds revealed that the amylose-zein interaction inhibited water permeation into the amylose cavity, leading to enhanced conformational stabilities of the V-type helical structure of amylose and the amylose-zein complexes. Furthermore, the amylose in amylose-zein complexes displayed the thermodynamically stable
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