1. Synthesis, α-glucosidase inhibitory and molecular docking studies of prenylated and geranylated flavones, isoflavones and chalcones
- Author
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Yashan Li, Tao Zhu, Xiaotong Song, Haomeng Wang, Yong-Min Zhang, Runling Wang, Xiaoting Zhang, Ying Ma, Xue Zhao, Hua Sun, Weina Ding, Yanan Lei, Qingwei Yao, Peng Yu, Tianjin University of Science and Technology, Glycochimie Organique Biologique et Supramoléculaire (GOBS), Institut Parisien de Chimie Moléculaire (IPCM), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Tianjin Medical University, and Institut de Chimie du CNRS (INC)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
Chalcone ,Stereochemistry ,Clinical Biochemistry ,Flavonoid ,Pharmaceutical Science ,010402 general chemistry ,01 natural sciences ,Biochemistry ,Flavones ,Molecular Docking Simulation ,Structure-Activity Relationship ,chemistry.chemical_compound ,Chalcones ,Drug Discovery ,Humans ,[CHIM]Chemical Sciences ,Structure–activity relationship ,Glycoside Hydrolase Inhibitors ,Molecular Biology ,IC50 ,ComputingMilieux_MISCELLANEOUS ,chemistry.chemical_classification ,Dose-Response Relationship, Drug ,Molecular Structure ,biology ,010405 organic chemistry ,Organic Chemistry ,Active site ,alpha-Glucosidases ,Isoflavones ,0104 chemical sciences ,chemistry ,biology.protein ,Molecular Medicine - Abstract
Three series of prenylated and/or geranylated flavonoids were synthesized and evaluated for their α-glucosidase inhibitory activity. The 3',5'-digeranylated chalcone (16) was identified as a new α-glucosidase inhibitor whose activity (IC50=0.90 μM) was 50-fold more than that of acarbose (IC50=51.32 μM). Molecular docking studies revealed the existence of strong hydrophobic interaction and H-bonding between compound 16 and α-glucosidase's active site. The inhibitory mode analysis showed that 16 exhibited a competitive inhibitory mode.
- Published
- 2015