(−)-Epicatechin derivate from Orostachys japonicus as potential inhibitor of the human butyrylcholinesterase

Jang Hoon Kim; Sang Hyun Lee; Hyun Woo Lee; Ya Nan Sun; Won Hee Jang; Seo Young Yang; Hae Dong Jang; Young Ho Kim

doi:10.1016/j.ijbiomac.2016.06.069

(−)-Epicatechin derivate from Orostachys japonicus as potential inhibitor of the human butyrylcholinesterase

Jang Hoon Kim, Sang Hyun Lee, Hyun Woo Lee, Ya Nan Sun, Won Hee Jang, Seo Young Yang, Hae Dong Jang, Young Ho Kim

Department of Biology Education

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

27 Scopus citations

Abstract

Cholinesterase inhibitors block the bioconversion of neurotransmitters by cholinesterase in the nervous system. Epicatechin derivatives (1, 3 and 5), polyphenols (6 and 7) from Orostachys japonicus, and catechin derivatives (2 and 4) from our in-house library were evaluated for their inhibitory activity on cholinesterase. Compound 5 exhibited IC₅₀ values of 58.3 ± 2.4 and 17.8 ± 3.8 μg/mL on AChE and BuChE, respectively. Compound 5 inhibited BuChE more strongly than AChE through a competitive behavior. In silico binding positions of 5 in the active site were predicted using Autodock 4.2 and processed in a 10000-ps molecular dynamics simulation to assess the stability of compound 5 binding.

Original language	English
Pages (from-to)	1033-1039
Number of pages	7
Journal	International Journal of Biological Macromolecules
Volume	91
DOIs	https://doi.org/10.1016/j.ijbiomac.2016.06.069
State	Published - 1 Oct 2016

Keywords

Cholinesterase
Competitive inhibitor
Crassulaceae
Molecular dymanics
Orostachys japonicus A. berger

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10.1016/j.ijbiomac.2016.06.069

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title = "(−)-Epicatechin derivate from Orostachys japonicus as potential inhibitor of the human butyrylcholinesterase",

abstract = "Cholinesterase inhibitors block the bioconversion of neurotransmitters by cholinesterase in the nervous system. Epicatechin derivatives (1, 3 and 5), polyphenols (6 and 7) from Orostachys japonicus, and catechin derivatives (2 and 4) from our in-house library were evaluated for their inhibitory activity on cholinesterase. Compound 5 exhibited IC50 values of 58.3 ± 2.4 and 17.8 ± 3.8 μg/mL on AChE and BuChE, respectively. Compound 5 inhibited BuChE more strongly than AChE through a competitive behavior. In silico binding positions of 5 in the active site were predicted using Autodock 4.2 and processed in a 10000-ps molecular dynamics simulation to assess the stability of compound 5 binding.",

keywords = "Cholinesterase, Competitive inhibitor, Crassulaceae, Molecular dymanics, Orostachys japonicus A. berger",

author = "Kim, {Jang Hoon} and Lee, {Sang Hyun} and Lee, {Hyun Woo} and Sun, {Ya Nan} and Jang, {Won Hee} and Yang, {Seo Young} and Jang, {Hae Dong} and Kim, {Young Ho}",

note = "Publisher Copyright: {\textcopyright} 2016 Elsevier B.V.",

year = "2016",

month = oct,

day = "1",

doi = "10.1016/j.ijbiomac.2016.06.069",

language = "English",

volume = "91",

pages = "1033--1039",

journal = "International Journal of Biological Macromolecules",

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T1 - (−)-Epicatechin derivate from Orostachys japonicus as potential inhibitor of the human butyrylcholinesterase

AU - Kim, Jang Hoon

AU - Lee, Sang Hyun

AU - Lee, Hyun Woo

AU - Sun, Ya Nan

AU - Jang, Won Hee

AU - Yang, Seo Young

AU - Jang, Hae Dong

AU - Kim, Young Ho

PY - 2016/10/1

Y1 - 2016/10/1

N2 - Cholinesterase inhibitors block the bioconversion of neurotransmitters by cholinesterase in the nervous system. Epicatechin derivatives (1, 3 and 5), polyphenols (6 and 7) from Orostachys japonicus, and catechin derivatives (2 and 4) from our in-house library were evaluated for their inhibitory activity on cholinesterase. Compound 5 exhibited IC50 values of 58.3 ± 2.4 and 17.8 ± 3.8 μg/mL on AChE and BuChE, respectively. Compound 5 inhibited BuChE more strongly than AChE through a competitive behavior. In silico binding positions of 5 in the active site were predicted using Autodock 4.2 and processed in a 10000-ps molecular dynamics simulation to assess the stability of compound 5 binding.

AB - Cholinesterase inhibitors block the bioconversion of neurotransmitters by cholinesterase in the nervous system. Epicatechin derivatives (1, 3 and 5), polyphenols (6 and 7) from Orostachys japonicus, and catechin derivatives (2 and 4) from our in-house library were evaluated for their inhibitory activity on cholinesterase. Compound 5 exhibited IC50 values of 58.3 ± 2.4 and 17.8 ± 3.8 μg/mL on AChE and BuChE, respectively. Compound 5 inhibited BuChE more strongly than AChE through a competitive behavior. In silico binding positions of 5 in the active site were predicted using Autodock 4.2 and processed in a 10000-ps molecular dynamics simulation to assess the stability of compound 5 binding.

KW - Cholinesterase

KW - Competitive inhibitor

KW - Crassulaceae

KW - Molecular dymanics

KW - Orostachys japonicus A. berger

UR - http://www.scopus.com/inward/record.url?scp=84976873404&partnerID=8YFLogxK

U2 - 10.1016/j.ijbiomac.2016.06.069

DO - 10.1016/j.ijbiomac.2016.06.069

M3 - Article

C2 - 27341781

AN - SCOPUS:84976873404

SN - 0141-8130

VL - 91

SP - 1033

EP - 1039

JO - International Journal of Biological Macromolecules

JF - International Journal of Biological Macromolecules

ER -

(−)-Epicatechin derivate from Orostachys japonicus as potential inhibitor of the human butyrylcholinesterase

Abstract

Keywords

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