Catechol derivatives inhibit the fibril formation of amyloid-β peptides

Vu Thi Huong; Toshinori Shimanouchi; Naoya Shimauchi; Hisashi Yagi; Hiroshi Umakoshi; Yuji Goto; Ryoichi Kuboi

doi:10.1016/j.jbiosc.2009.11.010

Catechol derivatives inhibit the fibril formation of amyloid-β peptides

Vu Thi Huong, Toshinori Shimanouchi, Naoya Shimauchi, Hisashi Yagi, Hiroshi Umakoshi, Yuji Goto, Ryoichi Kuboi

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

32 Citations (Scopus)

Abstract

The inhibition of fibril formation of amyloid β proteins (Aβ) would be attractive therapeutic targets for the treatment of Alzheimer's disease (AD). Dopamine (DA) and other catechol derivatives were used as inhibitory factors for Aβ fibril formation. The fibril formation of Aβ was monitored by Thioflavin T fluorescence, a transmission electron microscopy (TEM) and a total internal reflection fluorescence microscopy (TIRFM). Catechol and its derivatives showed the dose-dependent inhibitory effects on the spontaneous Aβ fibril formation. The inhibitory activity depended on the chemical structure of catechol derivatives both in the presence and absence of the liposome a model of biomembrane. Formation of catechol quinone-conjugated-Aβ adduct by a Schiff-base is a key step for the inhibition effect of Aβ fibril formation.

Original language	English
Pages (from-to)	629-634
Number of pages	6
Journal	Journal of Bioscience and Bioengineering
Volume	109
Issue number	6
DOIs	https://doi.org/10.1016/j.jbiosc.2009.11.010
Publication status	Published - Jun 2010
Externally published	Yes

Keywords

Alzheimer's disease
Amyloid beta
Catechol derivatives
Fibril formation
Inhibitor
Liposome

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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title = "Catechol derivatives inhibit the fibril formation of amyloid-β peptides",

abstract = "The inhibition of fibril formation of amyloid β proteins (Aβ) would be attractive therapeutic targets for the treatment of Alzheimer's disease (AD). Dopamine (DA) and other catechol derivatives were used as inhibitory factors for Aβ fibril formation. The fibril formation of Aβ was monitored by Thioflavin T fluorescence, a transmission electron microscopy (TEM) and a total internal reflection fluorescence microscopy (TIRFM). Catechol and its derivatives showed the dose-dependent inhibitory effects on the spontaneous Aβ fibril formation. The inhibitory activity depended on the chemical structure of catechol derivatives both in the presence and absence of the liposome a model of biomembrane. Formation of catechol quinone-conjugated-Aβ adduct by a Schiff-base is a key step for the inhibition effect of Aβ fibril formation.",

keywords = "Alzheimer's disease, Amyloid beta, Catechol derivatives, Fibril formation, Inhibitor, Liposome",

author = "Huong, {Vu Thi} and Toshinori Shimanouchi and Naoya Shimauchi and Hisashi Yagi and Hiroshi Umakoshi and Yuji Goto and Ryoichi Kuboi",

note = "Funding Information: The authors also thank the Grant-in-Aid for Scientific Research (No: 19566203 , 19656220 , 20760539 , 20360350 , 21246121 ) from the Ministry of Education, Science, Sports, and Culture of Japan, a grant from the 21st Century COE program “Creation of Integrated EcoChemistry” and the Global COE program “Bio-Environmental Chemistry” of JSPS. This work was also partly supported by the Core University Program between JSPS and Vietnamese Academy of Science and Technology (VAST). The authors are grateful to the Research Center for Solar Energy Chemistry of Osaka University and the Gas hydrate Analyzing System (Osaka University, Japan). A part of the present experiments was carried out by using a facility in the Research Center for Ultrahigh Voltage Electron Microscopy (Osaka University).",

year = "2010",

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doi = "10.1016/j.jbiosc.2009.11.010",

language = "English",

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AU - Huong, Vu Thi

AU - Shimanouchi, Toshinori

AU - Shimauchi, Naoya

AU - Yagi, Hisashi

AU - Umakoshi, Hiroshi

AU - Goto, Yuji

AU - Kuboi, Ryoichi

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PY - 2010/6

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KW - Alzheimer's disease

KW - Amyloid beta

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Catechol derivatives inhibit the fibril formation of amyloid-β peptides

Abstract

Keywords

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