Inhibitory activity of (−)-epicatechin-3,5-O-digallate on α-glucosidase and in silico analysis

Jang Hoon Kim; Hyo Young Kim; Seo Young Yang; Jin Baek Kim; Chang Hyun Jin; Young Ho Kim

doi:10.1016/j.ijbiomac.2017.09.091

Inhibitory activity of (−)-epicatechin-3,5-O-digallate on α-glucosidase and in silico analysis

Jang Hoon Kim, Hyo Young Kim, Seo Young Yang, Jin Baek Kim, Chang Hyun Jin, Young Ho Kim

Department of Biology Education

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

Abstract

(−)-Epicatechin-3,5-O-digallate (ECDG) from Orostachys japonicus A. Berger was examined for inhibitory activity on α-glucosidase. The results showed that the IC₅₀ value was achieved with nanomolar concentrations. Through the enzyme kinetic analysis, ECDG was shown to act as a competitive inhibitor of α-glucosidase by binding to the receptor active site. Fluorescence-quenching measurements showed that ECDG and the enzyme may have a one-to-one reaction with low quenching (K_sv) and binding constants. A molecular docking study was performed to evaluate the receptor-ligand complex. Asn236 was found to be particularly important for hydrogen bond formation during the molecular dynamics simulation.

Original language	English
Pages (from-to)	1162-1167
Number of pages	6
Journal	International Journal of Biological Macromolecules
Volume	107
Issue number	PartA
DOIs	https://doi.org/10.1016/j.ijbiomac.2017.09.091
State	Published - Feb 2018

Keywords

Competitive inhibitor
Epicatechin derivative
Molecular docking
Molecular dynamics
α-Glucosidase

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10.1016/j.ijbiomac.2017.09.091

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title = "Inhibitory activity of (−)-epicatechin-3,5-O-digallate on α-glucosidase and in silico analysis",

abstract = "(−)-Epicatechin-3,5-O-digallate (ECDG) from Orostachys japonicus A. Berger was examined for inhibitory activity on α-glucosidase. The results showed that the IC50 value was achieved with nanomolar concentrations. Through the enzyme kinetic analysis, ECDG was shown to act as a competitive inhibitor of α-glucosidase by binding to the receptor active site. Fluorescence-quenching measurements showed that ECDG and the enzyme may have a one-to-one reaction with low quenching (Ksv) and binding constants. A molecular docking study was performed to evaluate the receptor-ligand complex. Asn236 was found to be particularly important for hydrogen bond formation during the molecular dynamics simulation.",

keywords = "Competitive inhibitor, Epicatechin derivative, Molecular docking, Molecular dynamics, α-Glucosidase",

author = "Kim, \{Jang Hoon\} and Kim, \{Hyo Young\} and Yang, \{Seo Young\} and Kim, \{Jin Baek\} and Jin, \{Chang Hyun\} and Kim, \{Young Ho\}",

note = "Publisher Copyright: {\textcopyright} 2017",

year = "2018",

month = feb,

doi = "10.1016/j.ijbiomac.2017.09.091",

language = "English",

volume = "107",

pages = "1162--1167",

journal = "International Journal of Biological Macromolecules",

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TY - JOUR

T1 - Inhibitory activity of (−)-epicatechin-3,5-O-digallate on α-glucosidase and in silico analysis

AU - Kim, Jang Hoon

AU - Kim, Hyo Young

AU - Yang, Seo Young

AU - Kim, Jin Baek

AU - Jin, Chang Hyun

AU - Kim, Young Ho

PY - 2018/2

Y1 - 2018/2

N2 - (−)-Epicatechin-3,5-O-digallate (ECDG) from Orostachys japonicus A. Berger was examined for inhibitory activity on α-glucosidase. The results showed that the IC50 value was achieved with nanomolar concentrations. Through the enzyme kinetic analysis, ECDG was shown to act as a competitive inhibitor of α-glucosidase by binding to the receptor active site. Fluorescence-quenching measurements showed that ECDG and the enzyme may have a one-to-one reaction with low quenching (Ksv) and binding constants. A molecular docking study was performed to evaluate the receptor-ligand complex. Asn236 was found to be particularly important for hydrogen bond formation during the molecular dynamics simulation.

AB - (−)-Epicatechin-3,5-O-digallate (ECDG) from Orostachys japonicus A. Berger was examined for inhibitory activity on α-glucosidase. The results showed that the IC50 value was achieved with nanomolar concentrations. Through the enzyme kinetic analysis, ECDG was shown to act as a competitive inhibitor of α-glucosidase by binding to the receptor active site. Fluorescence-quenching measurements showed that ECDG and the enzyme may have a one-to-one reaction with low quenching (Ksv) and binding constants. A molecular docking study was performed to evaluate the receptor-ligand complex. Asn236 was found to be particularly important for hydrogen bond formation during the molecular dynamics simulation.

KW - Competitive inhibitor

KW - Epicatechin derivative

KW - Molecular docking

KW - Molecular dynamics

KW - α-Glucosidase

UR - https://www.scopus.com/pages/publications/85030786933

U2 - 10.1016/j.ijbiomac.2017.09.091

DO - 10.1016/j.ijbiomac.2017.09.091

M3 - Article

C2 - 28958819

AN - SCOPUS:85030786933

SN - 0141-8130

VL - 107

SP - 1162

EP - 1167

JO - International Journal of Biological Macromolecules

JF - International Journal of Biological Macromolecules

IS - PartA

ER -

Inhibitory activity of (−)-epicatechin-3,5-O-digallate on α-glucosidase and in silico analysis

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Keywords

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