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Enhanced cytotoxicity and antioxidant capacity of kaempferol complexed with α-lactalbumin.
Diao, Mengxue; Liang, Yuan; Zhao, Jingqi; Zhao, Changhui; Zhang, Jie; Zhang, Tiehua.
Afiliación
  • Diao M; College of Food Science and Engineering, Jilin University, Changchun, 130062, China.
  • Liang Y; College of Food Science and Engineering, Jilin University, Changchun, 130062, China.
  • Zhao J; College of Food Science and Engineering, Jilin University, Changchun, 130062, China.
  • Zhao C; College of Food Science and Engineering, Jilin University, Changchun, 130062, China.
  • Zhang J; College of Food Science and Engineering, Jilin University, Changchun, 130062, China. Electronic address: zhangjie83@jlu.edu.cn.
  • Zhang T; College of Food Science and Engineering, Jilin University, Changchun, 130062, China. Electronic address: zhangthjlu@163.com.
Food Chem Toxicol ; 153: 112265, 2021 Jul.
Article en En | MEDLINE | ID: mdl-34004225
ABSTRACT
As a dietary polyphenol, kaempferol exhibits numerous biological activities such as antioxidant and anticancer properties. However, its application is limited because of its poor solubility and low permeability. This work aims to investigate the interaction of kaempferol with α-lactalbumin. Multiple-spectroscopic techniques were used to prove the interaction between kaempferol and α-lactalbumin. UV-vis absorption spectra suggested that the conformation of α-lactalbumin could be changed via binding with kaempferol. The fluorescence quenching test showed that kaempferol significantly quenched the intrinsic fluorescence of α-lactalbumin. Circular dichroism spectroscopy showed that the percent helicity of α-lactalbumin secondary structure increased when combined with kaempferol. In addition, the α-lactalbumin-kaempferol complex showed stronger inhibition ability on the growth of HeLa cells compared with kaempferol alone. The complex also showed higher antioxidant capacity than kaempferol alone. Molecular docking provided three predicted binding sites of α-lactalbumin for kaempferol, as well as five predicted binding poses of kaempferol. The weak intermolecular interactions were the main forces to stabilize the α-lactalbumin-kaempferol complex. Besides, the binding stability between α-lactalbumin and kaempferol was explored by molecular dynamics simulation. In conclusion, this work provides a basis for the potential application of α-lactalbumin as a delivery carrier for kaempferol owing to its nontoxic and biocompatible properties.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Quempferoles / Lactalbúmina / Antioxidantes Límite: Animals / Humans Idioma: En Revista: Food Chem Toxicol Año: 2021 Tipo del documento: Article País de afiliación: China

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Quempferoles / Lactalbúmina / Antioxidantes Límite: Animals / Humans Idioma: En Revista: Food Chem Toxicol Año: 2021 Tipo del documento: Article País de afiliación: China