Abstract
The self-assembly behavior of proteins and peptides has been widely studied due to their ability to construct various nanostructures, such as nanotubes and nanofibrils. Understanding the self-assembly mechanism is of great significance for developing functional nanomaterials. Herein, we adopt a novel method to construct ovotransferrin (OVT) fibrils by subtilisin A hydrolysis and Ca2+ ions induced self-assembly with mild reaction conditions. The kinetic process of OVT fibrils formation contains lag, growth, and plateau stage. During the growth stage, OVT peptides self-assemble into precursor structures, which undergo morphological changes of twisted ribbons, helical ribbons, and nanotubes, ultimately closing to form mature fibrils. Ca2+ ions likely coordinate with the carboxyl groups of OVT peptides, aiding in the self-assembly process. And the secondary conformation is manifested as a β-sheet stacking. The mature OVT fibrils have distinct hollow and left-handed structures. Then OVT fibrils successfully encapsulate zeaxanthin (Zea) and improve its solubility and stability. Besides, OVT fibrils exhibit no in vitro cytotoxicity, and significantly reduce allergenicity to egg allergy patients compared to OVT. OVT fibrils delivery Zea into milk to develop Zea fortified dairy beverage and improve the viscosity of dairy beverage. OVT fibrils show a great potential as nutrient delivery and texture optimization for food application.
Published Version
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