title: Inhibitory mechanism of morin on α-glucosidase and its anti-glycation properties.
abstract: It is important to investigate the inhibition of α-glucosidase due to its correlation with type 2 diabetes. Morin was found to exert significant inhibition activity on α-glucosidase in a reversible mixed-type manner with an IC50 value of (4.48 ± 0.04) μM. Analyses of fluorescence and circular dichroism spectra indicated that the formation of the morin-α-glucosidase complex was driven mainly by hydrophobic forces and hydrogen bonding, and caused the conformational changes of α-glucosidase. The phase diagrams of fluorescence showed that the conformational change process was monophasic without intermediates. Molecular docking indicated that morin mainly interacted with amino acid residues located close to the active site of α-glucosidase, which may move to cover the active pocket to reduce the binding of the substrate and then inhibit the catalytic activity. Morin was also found to exhibit inhibition in the generation of advanced glycation end products which was related to the long term complications of diabetes.
authors.affiliation: State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China. gwzhang@ncu.edu.cn.
authors.forename: Li
authors.initials: L
authors.lastname: Zeng
authors.forename: Guowen
authors.initials: G
authors.lastname: Zhang
authors.forename: Yijing
authors.initials: Y
authors.lastname: Liao
authors.forename: Deming
authors.initials: D
authors.lastname: Gong
mesh_terms: D020909:Acarbose / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D000975:Antioxidants / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D001665:Binding Sites; D020134:Catalytic Domain; D002942:Circular Dichroism; D016000:Cluster Analysis; D019587:Dietary Supplements / Q000032:analysis; D005419:Flavonoids / Q000737:chemistry / Q000378:metabolism*; D005960:Glucosides / Q000737:chemistry / Q000378:metabolism; D017127:Glycation End Products, Advanced / Q000037:antagonists & inhibitors* / Q000378:metabolism; D065089:Glycoside Hydrolase Inhibitors / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D006031:Glycosylation / Q000187:drug effects; D006801:Humans; D007004:Hypoglycemic Agents / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D007700:Kinetics; D008968:Molecular Conformation; D062105:Molecular Docking Simulation; D029701:Saccharomyces cerevisiae Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D013816:Thermodynamics; D000520:alpha-Glucosidases / Q000737:chemistry / Q000378:metabolism; D047309:Flavones
chemical_list: D020909:Acarbose; D000975:Antioxidants; D005419:Flavonoids; D005960:Glucosides; D017127:Glycation End Products, Advanced; D065089:Glycoside Hydrolase Inhibitors; D007004:Hypoglycemic Agents; D029701:Saccharomyces cerevisiae Proteins; D000520:alpha-Glucosidases; C019502:4-nitrophenyl alpha-glucoside; C008548:morin; D047309:Flavones