New Insights into the Inhibition Mechanism of Betulinic Acid on α-Glucosidase

Ding, Huafang; Wu, Xia-Qing; Pan, Junhui; Hu, Xiaofeng; Gong, Deming; Zhang, Guowen

doi:10.1021/acs.jafc.8b02992

Cited by 148 publications

(79 citation statements)

References 53 publications

(103 reference statements)

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“…The values of K a and n at 298, 304, and 310 K were calculated with Eqn 6 (Table ). K a is the binding constant for the α ‐glucosidase–CRA complex, the order of magnitude of the K a values was 10 3 L mol −1 , indicating a moderate binding affinity in the binding reaction of CRA with α ‐glucosidase, which was consistent with the binding of betulinic acid to α ‐glucosidase determined by Ding et al . Recent studies by Zhang et al .…”

Section: Resultssupporting

confidence: 81%

“…The values of K a and n at 298, 304, and 310 K were calculated with Eqn 6 ( Table 2). K a is the binding constant for the -glucosidase-CRA complex, the order of magnitude of the K a values was 10 3 L mol −1 , indicating a moderate binding affinity in the binding reaction of CRA with -glucosidase, 18 which was consistent with the binding of betulinic acid to -glucosidase determined by Ding et al 44 Recent studies by Zhang et al had found that CRA had a high absorption rate in the stomach of rat and showed a good permeability in the intestine. Its effective permeability in the ileum at 9 μg/mL (1.91 × 10 −5 mol L −1 ) was remarkably higher than the IC 50 value of CRA on -glucosidase.…”

Section: Thermodynamic Parameterssupporting

confidence: 83%

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Inhibitory effect of corosolic acid on α‐glucosidase: kinetics, interaction mechanism, and molecular simulation

Pan

et al. 2019

J Sci Food Agric

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BACKGROUND The suppression of α‐glucosidase activity to retard glucose absorption is an important therapy for type‐2 diabetes. Corosolic acid (CRA) is a potential antidiabetic component in many plant‐based foods and herbs. In this study, the interplay mechanism between α‐glucosidase and corosolic acid was investigated by several methods, including three‐dimensional fluorescence spectra, circular dichroism spectra, and molecular simulation. RESULTS Corosolic acid significantly inhibited α‐glucosidase reversibly in an uncompetitive manner and its IC50 value was 1.35 × 10−5 mol L−1. A combination of CRA with myricetin exerted a weak synergy against α‐glucosidase. The intrinsic fluorescence of α‐glucosidase was quenched via a static quenching course and the binding constant was 3.47 × 103 L mol−1 at 298 K. The binding of CRA to α‐glucosidase was mainly driven by hydrophobic forces and resulted in a partial extension of the protein polypeptide chain with a loss of α‐helix content. The molecular simulation illustrated that CRA bound to the entrance part of the active center of α‐glucosidase and interacted with the amino acid residues Ser157, Arg442, Phe303, Arg315, Tyr158, and Gln353, which could hinder the release of substrate and catalytic reaction product, eventually suppressing the catalytic activity of α‐glucosidase. CONCLUSIONS These results may suggest new insights into corosolic acid from food sources as a potential α‐glucosidase inhibitor that could better control diabetes. © 2019 Society of Chemical Industry

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Section: Resultssupporting

confidence: 81%

Section: Thermodynamic Parameterssupporting

confidence: 83%

Inhibitory effect of corosolic acid on α‐glucosidase: kinetics, interaction mechanism, and molecular simulation

Pan

et al. 2019

J Sci Food Agric

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“…It was difficult to distinguish the spectra of 5‐HMF–ctDNA complex and judge whether the interaction between 5‐HMF and ctDNA occurred. Hence, the MCR‐ALS method was introduced to resolve the complex spectral data matrix to obtain detailed information of the 5‐HMF–ctDNA interaction …”

Section: Resultsmentioning

confidence: 99%

Exploring the binding interaction of Maillard reaction by‐product 5‐hydroxymethyl‐2‐furaldehyde with calf thymus DNA

Zhou

Zhang

et al. 2019

J Sci Food Agric

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BACKGROUND 5‐Hydroxymethyl‐2‐furaldehyde (5‐HMF), a by‐product of the Maillard reaction, usually present in fried and baked food, may cause potential harm to the human body. Here, the interaction between 5‐HMF and calf thymus DNA (ctDNA) under physiological buffer (pH 7.4) was studied using multi‐spectroscopic methods combined with multivariate curve resolution–alternating least squares (MCR‐ALS) chemometrics and molecular simulation techniques. RESULTS The concentration profiles and pure spectra of the three components (5‐HMF, ctDNA and 5‐HMF–ctDNA complex) were extracted from highly overlapping spectra using MCR‐ALS analysis, which verified the formation of 5‐HMF–ctDNA complex. The binding constant being of the order of 103 L mol−1 at four temperatures (292, 298, 304 and 310 K) indicated a weak affinity in the binding of 5‐HMF to ctDNA. The binding interaction was mainly driven by hydrogen bonds and van der Waals forces. Viscosity analysis, melting assay, ionic strength effect and competitive fluorescence studies ascertained that 5‐HMF bound to ctDNA through groove binding, and it tended to bind to guanine–cytosine rich region of ctDNA which was characterized using Fourier transform infrared spectra and molecular docking. Circular dichroism spectral analysis and DNA cleavage assays indicated that the ctDNA conformation was altered from B to A form and 5‐HMF caused DNA damage at higher concentration. CONCLUSIONS The results suggested that 5‐HMF bound to ctDNA through groove binding and caused DNA damage. This research may contribute to understand the binding mechanism of 5‐HMF to ctDNA and to the assessment of the toxicological effect of 5‐HMF in biological processes. © 2018 Society of Chemical Industry

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“…The CD spectra of SPI had one negative band at 216 nm due to the existence of β-sheet (Figure 2c; Ding et al, 2018). With increasing concentrations of TG (from 0 to 8.0 U/g) to SPI solution, a gradual lessening in the intensity of the negative band was observed, the contents of the α-helix and β-sheet decreased from 5.32% to 3.42% and 49.53% to 44.91%, respectively, whereas the contents of random and coil β-turn increased from 23.89% to 28.94% and 21.87%…”

Section: Secondary Structuresmentioning

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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New Insights into the Inhibition Mechanism of Betulinic Acid on α-Glucosidase

Cited by 148 publications

References 53 publications

Inhibitory effect of corosolic acid on α‐glucosidase: kinetics, interaction mechanism, and molecular simulation

Inhibitory effect of corosolic acid on α‐glucosidase: kinetics, interaction mechanism, and molecular simulation

Exploring the binding interaction of Maillard reaction by‐product 5‐hydroxymethyl‐2‐furaldehyde with calf thymus DNA

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

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