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Inhibition of α-glucosidase activity and non-enzymatic glycation by tannic acid: Inhibitory activity and molecular mechanism.
Huang, Qian; Chai, Wei-Ming; Ma, Zuo-Yuan; Ou-Yang, Chong; Wei, Qi-Ming; Song, Shuang; Zou, Zheng-Rong; Peng, Yi-Yuan.
Afiliación
  • Huang Q; College of Life Science and Key Laboratory of Functional Small Organic Molecule, Ministry of Education, Jiangxi Normal University, Nanchang, Jiangxi 330022, China.
  • Chai WM; College of Life Science and Key Laboratory of Functional Small Organic Molecule, Ministry of Education, Jiangxi Normal University, Nanchang, Jiangxi 330022, China. Electronic address: chaiweiming@jxnu.edu.cn.
  • Ma ZY; College of Life Science and Key Laboratory of Functional Small Organic Molecule, Ministry of Education, Jiangxi Normal University, Nanchang, Jiangxi 330022, China.
  • Ou-Yang C; College of Life Science and Key Laboratory of Functional Small Organic Molecule, Ministry of Education, Jiangxi Normal University, Nanchang, Jiangxi 330022, China.
  • Wei QM; College of Life Science and Key Laboratory of Functional Small Organic Molecule, Ministry of Education, Jiangxi Normal University, Nanchang, Jiangxi 330022, China.
  • Song S; College of Life Science and Key Laboratory of Functional Small Organic Molecule, Ministry of Education, Jiangxi Normal University, Nanchang, Jiangxi 330022, China.
  • Zou ZR; College of Life Science and Key Laboratory of Functional Small Organic Molecule, Ministry of Education, Jiangxi Normal University, Nanchang, Jiangxi 330022, China.
  • Peng YY; College of Life Science and Key Laboratory of Functional Small Organic Molecule, Ministry of Education, Jiangxi Normal University, Nanchang, Jiangxi 330022, China.
Int J Biol Macromol ; 141: 358-368, 2019 Dec 01.
Article en En | MEDLINE | ID: mdl-31491512
The inhibition of α-glucosidase and glycation is considered as an effective approach for the treatment of type 2 diabetes. In this study, multispectroscopic and molecular docking techniques were employed to investigate the inhibition of tannic acid on α-glucosidase and glycation. Kinetics analyses revealed that tannic acid had a significant inhibition on α-glucosidase (IC50 = 0.35 ±â€¯0.02 µM) in a reversible and mixed competitive manner. The results acquired from fluorescence quenching and ANS-binding fluorescence methods revealed that tannic acid could bind to α-glucosidase and reduce the hydrophobic area on the surface of the enzyme. In addition, synchronous fluorescence analysis showed that tannic acid decreased the hydrophobicity of α-glucosidase and changed the conformation of the enzyme. In vitro glycation assays showed that tannic acid had strong inhibitory effects on the formation of fructosamine, dicarbonyl compounds, and fluorescent AGEs. ANS-binding fluorescence analysis showed that tannic acid could bind to BSA and reduce the hydrophobicity of BSA in glycation. Moreover, the results of molecular docking showed the interaction between tannic acid and α-glucosidase was mainly driven by hydrogen bond, electrostatic, and hydrophobic interaction. And the interaction between tannic acid and BSA was mainly driven by hydrogen bond and hydrophobic interaction.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Taninos / Alfa-Glucosidasas / Inhibidores de Glicósido Hidrolasas Idioma: En Revista: Int J Biol Macromol Año: 2019 Tipo del documento: Article País de afiliación: China Pais de publicación: Países Bajos
Texto completo
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XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Taninos / Alfa-Glucosidasas / Inhibidores de Glicósido Hidrolasas Idioma: En Revista: Int J Biol Macromol Año: 2019 Tipo del documento: Article País de afiliación: China Pais de publicación: Países Bajos