Inhibitory effects of epigallocatechin gallate and its glucoside on the human intestinal maltase inhibition

Nguyen, Thi Thanh Hanh; Jung, Sang-Don; Lee, Sun; Ryu, Hwa-Ja; Kang, Hee-Kyoung; Moon, Yea Hwang; Kim, Young‐Min; Kimura, Atsuo; Kim, Doman

doi:10.1007/s12257-012-0242-8

Cited by 21 publications

(20 citation statements)

References 34 publications

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“…These data show that the ligand binds in a region of the protein mainly composed by aromatic and hydrophilic side chains, forming a combination of hydrophobic interactions and hydrogen bonds that favored the binding. Different types of interactions have been reported for EGCG with other proteins such as human salivary α-amylase, 48 human intestinal maltase, 49 and amyloid-β, 50 which shows that EGCG binding for each system has a different nature. Among the preferred docking poses, Y37, Y50, and Q92 repeatedly play an important role interacting with the ligand.…”

Section: ■ Discussionmentioning

confidence: 99%

Inhibition of Light Chain 6aJL2-R24G Amyloid Fiber Formation Associated with Light Chain Amyloidosis

et al. 2015

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Light chain amyloidosis (AL) is a deadly disease characterized by the deposition of monoclonal immunoglobulin light chains as insoluble amyloid fibrils in different organs and tissues. Germ line λ VI has been closely related to this condition; moreover, the R24G mutation is present in 25% of the proteins of this germ line in AL patients. In this work, five small molecules were tested as inhibitors of the formation of amyloid fibrils from the 6aJL2-R24G protein. We have found by thioflavin T fluorescence and transmission electron microscopy that EGCG inhibits 6aJL2-R24G fibrillogenesis. Furthermore, using nuclear magnetic resonance spectroscopy, dynamic light scattering, and isothermal titration calorimetry, we have determined that the inhibition is due to binding to the protein in its native state, interacting mainly with aromatic residues.

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Section: ■ Discussionmentioning

confidence: 99%

Inhibition of Light Chain 6aJL2-R24G Amyloid Fiber Formation Associated with Light Chain Amyloidosis

et al. 2015

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“…Our previous results indicated that B2-3’- O -gallate ( K i = 0.30 ± 0.03 μM, K i’ = 1.42 ± 0.01 μM), ECG ( K i = 0.21 ± 0.04 μM, K i’ = 2.34 ± 0.06 μM), and quercetin ( K i = 1.44 ± 0.04 μM, K i’ = 9.33 ± 0.10 μM) were mixed-competitive inhibitors of α-glucosidase [15]. Furthermore, a Lineweaver–Burk plot indicated that epigallocatechin gallate was a competitive inhibitor against maltose substrate for maltase, and the K i calculated from a Dixon plot was 5.93 ± 0.26 µM [25].…”

Section: Resultsmentioning

confidence: 99%

Characterization of Maltase and Sucrase Inhibitory Constituents from Rhodiola crenulata

Chuang

Hsieh

2019

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The inhibitory properties of epicatechin-(4β,8)-epicatechingallate (B2-3’-O-gallate), epicatechin gallate (ECG), and epicatechin (EC) isolated from Rhodiola crenulata toward maltase and sucrase were investigated. The half-maximal inhibitory concentration (IC50) values for maltase were as follows: B2-3’-O-gallate (1.73 ± 1.37 μM), ECG (3.64 ± 2.99 μM), and EC (6.25 ± 1.84 μM). Inhibition kinetic assays revealed the inhibition constants (Ki) of the mixed-competitive inhibitors of maltase, as follows: B2-3’-O-gallate (1.99 ± 0.02 μM), ECG (3.14 ± 0.04 μM), and EC (7.02 ± 0.26 μM). These compounds also showed a strong inhibitory activity toward sucrase, and the IC50 values of B2-3’-O-gallate, ECG, and EC were 6.91 ± 3.41, 18.27 ± 3.99, and 18.91 ± 3.66 μM, respectively. Inhibition kinetic assays revealed the inhibition constants (Ki) of the mixed-competitive inhibitors of sucrase as follows: B2-3’-O-gallate (6.05 ± 0.04 μM), ECG (8.58 ± 0.08 μM), and EC (13.72 ± 0.15 μM). Overall, these results suggest that B2-3’-O-gallate, ECG, and EC are potent maltase and sucrase inhibitors.

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“…The three-dimensional coordinates in the X-ray crystal structure of NS3 pro (PDB accession number 2VBC) [27] obtained from the Protein Data Bank [26,31] were used as the receptor model for the structural-based VS docking simulations. The NS3 pro docking library comprised 300,000 compounds from ChemDiv Inc. (San Diego, CA, USA), a commercially available compound library, was used for VS. AutoDock version 3.0.5 was used for the computational molecular docking simulation of flexible small molecules to rigid proteins using ligand and rigid proteins [32,33]. Large-scale computations were conducted between 2VBC and 300,000 compounds using the GVSS [26].…”

Section: Methodsmentioning

confidence: 99%

In Vitro Evaluation of Novel Inhibitors against the NS2B-NS3 Protease of Dengue Fever Virus Type 4

et al. 2013

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Abstract:The discovery of potent therapeutic compounds against dengue virus is urgently needed. The NS2B-NS3 protease (NS2B-NS3 pro ) of dengue fever virus carries out all enzymatic activities needed for polyprotein processing and is considered to be amenable to antiviral inhibition by analogy. Virtual screening of 300,000 compounds using Autodock 3 on the GVSS platform was conducted to identify novel inhibitors against the NS2B-NS3 pro . Thirty-six compounds were selected for in vitro assay against NS2B-NS3 pro expressed in Pichia pastoris. Seven novel compounds were identified as inhibitors with IC 50 values of 3.9 ± 0.6-86.7 ± 3.6 μM. Three strong NS2B-NS3 pro inhibitors were further confirmed as competitive inhibitors with K i values of 4.0 ± 0.4, 4.9 ± 0.3, and 3.4 ± 0.1 μM, respectively. Hydrophobic and hydrogen bond interactions between amino acid residues in the NS3 pro active site with inhibition compounds were also identified.

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Inhibitory effects of epigallocatechin gallate and its glucoside on the human intestinal maltase inhibition

Cited by 21 publications

References 34 publications

Inhibition of Light Chain 6aJL2-R24G Amyloid Fiber Formation Associated with Light Chain Amyloidosis

Inhibition of Light Chain 6aJL2-R24G Amyloid Fiber Formation Associated with Light Chain Amyloidosis

Characterization of Maltase and Sucrase Inhibitory Constituents from Rhodiola crenulata

In Vitro Evaluation of Novel Inhibitors against the NS2B-NS3 Protease of Dengue Fever Virus Type 4

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