• DOI:10.1021/acs.jafc.0c01191
• Corpus ID: 219726937

Double interfaces binding of two bioactive compounds with a cage-like ferritin.

@article{Meng2020DoubleIB,
  title={Double interfaces binding of two bioactive compounds with a cage-like ferritin.},
  author={Demei Meng and Shengnan Chen and Jie Liu and Qiao'e Wang and Desheng Wang and Mengyao Liu and Zhongkai Zhou and Rui Yang},
  journal={Journal of agricultural and food chemistry},
  year={2020}
}

• Demei Meng, Shengnan Chen, +5 authors Rui Yang
• Published 16 June 2020
• Biology, Chemistry
• Journal of agricultural and food chemistry

Ferritin is a cage-like carrier protein with multiple interfaces, allowing the encapsulation and delivery of biologically active molecules. In this study, hesperetin was covalently conjugated to the outer surface of ferritin to fabricate hesperetin-covalently modified ferritin (HFRT) at pH 9.0. This conjugation resulted in a binding equivalent of hesperetin to ferritin of 12.33±0.56 nmol/mg. After covalent binding, the free amino content of HFRT decreased, and the secondary and tertiary structures of HFRT were changed relative to the structure of control ferritin. In addition, HFRT successfully retained the cage-like structure of ferritin and exhibited reversible self-assembly property regulated by pH shifts. Taking advantage of this property, quercetin was encapsulated into the inner surface of HFRT with an encapsulation ratio of 14.0±1.36% (w/w). The modification with hesperetin improved the digestive stability of ferritin, and enhanced the stability of the encapsulated quercetin against thermal treatment compared to the unmodified one. This study explored the functions of the double interfaces of ferritin by covalent and non-covalent binding of two different bioactive compounds. The results can help guide the functionalization of the ferritin cage as a nanocarrier in food application.