Galangin inhibits α-glucosidase activity and formation of non-enzymatic glycation products

Zeng, Li; Ding, Huafang; Hu, Xiaofeng; Zhang, Guowen; Gong, Deming

doi:10.1016/j.foodchem.2018.07.148

Cited by 172 publications

(97 citation statements)

References 40 publications

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“…Many studies also verified that Asp 215 and Glu 411 were the important active sites involved in this catalytic reaction [28,34]. In addition, the formation of hydrogen bonds between the hydroxyl group at C-3 or C-4 of the molecules (i.e., quercetin and rutin) and the active site residues may produce a higher inhibitory ability towards α-glucosidase compared to kaempferol-3-O-rutinoside, which was consistent with the results reported by Zeng et al (2016) [41]. Rasouli et al (2017) also reported that the hydrogen bonds and active site residues formed by the ligand molecules and receptor enzymes exerted important effects on α-glucosidase inhibitory activities [42].…”

Section: Molecular Docking Analysissupporting

confidence: 89%

Free and Bound Phenolics of Buckwheat Varieties: HPLC Characterization, Antioxidant Activity, and Inhibitory Potency towards α-Glucosidase with Molecular Docking Analysis

et al. 2019

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Free and bound phenolic fractions from six buckwheat varieties were investigated for their compositions, antioxidant activities, and inhibitory effects on α-glucosidase. The results showed that different buckwheat varieties have significant differences in phenolic/flavonoid contents, and these contents were found in higher quantities in free form than in bound form. HPLC results revealed that rutin, quercetin, and kaempferol-3-O-rutinoside were the most abundant components in free and bound forms, whereas dihydromyricetin was found only in the bound form. Free phenolics showed higher antioxidant activities of DPPH, ABTS+, OH•, and FRAP than those of bound phenolics. Strong inhibitory effects against α-glucosidase by the free/bound phenolic fractions were found in all buckwheat varieties, and free phenolics showed stronger α-glucosidase inhibition than that of the corresponding bound phenolics. More importantly, the main phenolic compounds observed in the buckwheat varieties were subjected to molecular docking analysis to provide insight into their interactions with α-glucosidase. The contributions by individual phenolics to the observed variation was analysed by Pearson correlation coefficient analysis and principal component analysis. The present study provides a comprehensive comparison for the phenolic fractions of buckwheat varieties and identify the main contributors to antioxidant and α-glucosidase inhibitory activity.

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Section: Molecular Docking Analysissupporting

confidence: 89%

Free and Bound Phenolics of Buckwheat Varieties: HPLC Characterization, Antioxidant Activity, and Inhibitory Potency towards α-Glucosidase with Molecular Docking Analysis

et al. 2019

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“…Keeping the concentration of SPI at 0.2 mg/ml, and the weight ratios of TG to SPI were 0, 0.2%, 0.4%, 0.6%, and 0.8%, respectively. The contents of different secondary structures of SPI were determined from CD spectroscopic data by the online SELCON3 program (http://dichroweb.cryst.bbk.ac.uk/html/home.shtml; Zeng, Ding, Hu, Zhang, & Gong, ).…”

Section: Methodsmentioning

confidence: 99%

Influence of transglutaminase‐assisted ultrasound treatment on the structure and functional properties of soy protein isolate

Xinyue

Zeng

Zhang

et al. 2019

J Food Process Preserv

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In this study, the effects of transglutaminase (TG) cross‐linking on physicochemical, conformational, and functional properties of soybean protein isolate (SPI) with or without ultrasound pretreatment were investigated. Electrophoresis and free amino group analysis confirmed that the SPI was cross‐linked by TG treatment. The cross‐linked SPI showed a visible decrease in solubility and increase in apparent viscosity compared with the untreated SPI. TG catalyzed the SPI to unfold the constitutive polypeptides, resulting in a more random secondary structure. With ultrasound pretreatment, the cross‐linked SPI exhibited higher solubility (from 41.80% to 54.42%), emulsifying activity index (from 45.82 to 64.10 m2/g) and better foaming capacity (from 31.81% to 44.23%) than the untreated SPI, and the sulfhydryl group contents and surface hydrophobicity of the SPI were increased. Practical applications This study aimed to explore the effect of TG cross‐linking with or without ultrasound pretreatment on the physicochemical structure and functional properties of commercial SPI. The results demonstrated that a combination of ultrasound and TG treatments may be a valid way for the functional modification of SPI, which would be conducive to enhance its application as a novel functional ingredient in a broad range of food systems.

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“…Plenty of natural a-glucosidase inhibitors, e.g., luteolin, genistein, morin and galangin, were all reported to work in a mixed-type manner. 5,41,58 Such dietary avonoids could form enzymeinhibitor complexes as well as enzyme-substrate-inhibitor complexes to interrupt enzyme-substrate intermediate. 58…”

Section: Kinetic Type Of Inhibition On A-glucosidasementioning

confidence: 99%

“…where F 0 , F and [Q] denoted the same as eqn (5). K a represented binding constant of avonol and a-glucosidase.…”

Section: Fluorescence Quenching Studies and Binding Parametersmentioning

confidence: 99%

“…4 Inhibition of a-glucosidase is an effective way for treatment of T2D by delaying the release of glucose and alleviating postprandial hyperglycemia. 5 Drugs such as acarbose, miglitol, and voglibose are clinically used as a-glucosidase inhibitors for treatment of T2D. However, these drugs cause side effects such as gastrointestinal adverse reaction including diarrhea, atulence, abdominal pain and so on.…”

Section: Introductionmentioning

confidence: 99%

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α-Glucosidase inhibitors from Chinese bayberry (Morella rubraSieb. et Zucc.) fruit: molecular docking and interaction mechanism of flavonols with different B-ring hydroxylations

Liu

Zhan

et al. 2020

RSC Adv.

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Galangin inhibits α-glucosidase activity and formation of non-enzymatic glycation products

Cited by 172 publications

References 40 publications

Free and Bound Phenolics of Buckwheat Varieties: HPLC Characterization, Antioxidant Activity, and Inhibitory Potency towards α-Glucosidase with Molecular Docking Analysis

Free and Bound Phenolics of Buckwheat Varieties: HPLC Characterization, Antioxidant Activity, and Inhibitory Potency towards α-Glucosidase with Molecular Docking Analysis

Influence of transglutaminase‐assisted ultrasound treatment on the structure and functional properties of soy protein isolate

α-Glucosidase inhibitors from Chinese bayberry (Morella rubraSieb. et Zucc.) fruit: molecular docking and interaction mechanism of flavonols with different B-ring hydroxylations

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