Inhibition of human α-amylase by dietary polyphenols

Nyambe-Silavwe, Hilda; Villa-Rodríguez, José A.; Ifie, Idolo; Holmes, Melvin; Aydin, Ebru; Jensen, Jim; Williamson, Gary

doi:10.1016/j.jff.2015.10.003

Cited by 134 publications

(109 citation statements)

References 36 publications

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“…Conversely, Nyambe‐Silavwe et al. () used a concentration interval closer to that of the present study (5 to 70 μM compared with 1 to 7.5 μM). It seems therefore that the inhibition profile of these alpha‐amylases by flavanols rather depends on the experimental conditions, especially the concentration of the inhibitor and the degree of purity of the enzyme.…”

Section: Resultsmentioning

confidence: 62%

“…Lastly, it is worth mentioning that the HSA catalyzed hydrolysis of amylopectin—the main constituent of most starches—is inhibited by EGCG, acarbose, quercetin, luteolin, and green tea with a IC 50 comprised between 10 μM (acarbose) and 83 μM (quercetin). Similarly, with the HSA/amylose couple, IC 50 is comprised between 3.5 μM (acarbose) and 26.3 μM (luteolin) (Nyambe‐Silavwe et al., ). Thus, overall, these five HSA inhibitors are 3‐ to 10‐fold more effective on the amylose hydrolysis than on the amylopectin hydrolysis.…”

Section: Resultsmentioning

confidence: 99%

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The Mechanisms of Alpha‐Amylase Inhibition by Flavan‐3‐Ols and the Possible Impacts of Drinking Green Tea on Starch Digestion

Desseaux

Stocker

Brouant

et al. 2018

Journal of Food Science

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Many studies have shown that flavan‐3‐ols inhibit mammalian alpha‐amylases but the published IC50 and Ki values vary up to a thousand times. We therefore tested the effects of 6 pure flavan‐3‐ols—abundant in green tea—on the activity of pure porcine pancreatic alpha‐amylase (PPA) under steady‐state kinetic conditions. We used both amylose and maltopentaose as substrates, along with spectrophotometry and chromatography as analytical tools, respectively. A Docking approach was also used to probe the interaction between PPA and each flavan‐3‐ol. The results showed that the 6 flavan‐3‐ols inhibit amylose hydrolysis with Ki comprised between 7 and 34 μM, according to a mixed inhibition profile for gallocatechin gallate, and a competitive inhibition profile for the 5 other flavanols. Only the galloyl‐containing flavan‐3‐ols inhibited the maltopentaose hydrolysis with a Ki of about 30 μM according to a noncompetitive profile. We conclude that dietary flavan‐3‐ols could inhibit starch digestion nonnegligibly. The results of the docking trials were concordant with the kinetic data and have noticeably revealed that the cis‐flavan‐3‐ols epigallocatechin gallate and epicatechin gallate bind similarly to PPA, involving π‐stacking with Trp59.

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Section: Resultsmentioning

confidence: 62%

Section: Resultsmentioning

confidence: 99%

The Mechanisms of Alpha‐Amylase Inhibition by Flavan‐3‐Ols and the Possible Impacts of Drinking Green Tea on Starch Digestion

Desseaux

Stocker

Brouant

et al. 2018

Journal of Food Science

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“…The maximum DMSO concentration (5%) in the assay did not affect the enzyme activity as assessed in control incubations. Inhibition of human salivary α‐amylase was tested as previously described . Maltase, sucrase and isomaltase assays were conducted as before with some modifications.…”

Section: Methodsmentioning

confidence: 99%

Green and Chamomile Teas, but not Acarbose, Attenuate Glucose and Fructose Transport via Inhibition of GLUT2 and GLUT5

Villa-Rodríguez

Aydin

Gauer

et al. 2017

Molecular Nutrition Food Res

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“…The effect of on α-amylase (EC 3.2.1.1) activity was determined according to the method described in protocol 16,17 with some modification. Preliminary experiments were conducted to establish optimal assay conditions such as temperature, substrate enzyme and inhibitor concentration.…”

Section: Anti-diabetic Activitymentioning

confidence: 99%

Synthesis, Characterization, In Vitro Anti-diabetic, Antibacterial and Anticorrosive Activity of Some Cr(III) Complexes of Schiff Bases Derived from Isoniazid

2018

Chem Sci Trans

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Four complexes of Cr(III) were synthesized with Schiff bases ligands derived from isonicotinyl hydrazide with benzaldehyde/ p-chlorobenzaldehyde. The ligands and complexes were characterized by elemental analysis, molar conductance, magnetic moment, FT-IR, 1 H NMR, 13 C{ 1 H} NMR and electronic spectroscopy. The molecular structure and different quantum chemical parameters such as dipole moment and polarizability, were calculated using the B3LYP basis set density functional theory (DFT) with the standard 6-311+G(d, 2p) level. The calculated HOMO and LUMO energies show that charge transfer occurs within the molecules. Ligands and complexes were screened for in vitro anti-diabetic and antibacterial activity. Anticorrosion activity of complexes was also studied by weight loss method.

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Inhibition of human α-amylase by dietary polyphenols

Cited by 134 publications

References 36 publications

The Mechanisms of Alpha‐Amylase Inhibition by Flavan‐3‐Ols and the Possible Impacts of Drinking Green Tea on Starch Digestion

The Mechanisms of Alpha‐Amylase Inhibition by Flavan‐3‐Ols and the Possible Impacts of Drinking Green Tea on Starch Digestion

Green and Chamomile Teas, but not Acarbose, Attenuate Glucose and Fructose Transport via Inhibition of GLUT2 and GLUT5

Synthesis, Characterization, In Vitro Anti-diabetic, Antibacterial and Anticorrosive Activity of Some Cr(III) Complexes of Schiff Bases Derived from Isoniazid

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