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 | |
| Publication status | Published - Jun 2010 |
| Externally published | Yes |
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Keywords
- Alzheimer's disease
- Amyloid beta
- Catechol derivatives
- Fibril formation
- Inhibitor
- Liposome
ASJC Scopus subject areas
- Biotechnology
- Applied Microbiology and Biotechnology
- Bioengineering
Cite this
Catechol derivatives inhibit the fibril formation of amyloid-β peptides. / Huong, Vu Thi; Shimanouchi, Toshinori; Shimauchi, Naoya; Yagi, Hisashi; Umakoshi, Hiroshi; Goto, Yuji; Kuboi, Ryoichi.
In: Journal of Bioscience and Bioengineering, Vol. 109, No. 6, 06.2010, p. 629-634.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Catechol derivatives inhibit the fibril formation of amyloid-β peptides
AU - Huong, Vu Thi
AU - Shimanouchi, Toshinori
AU - Shimauchi, Naoya
AU - Yagi, Hisashi
AU - Umakoshi, Hiroshi
AU - Goto, Yuji
AU - Kuboi, Ryoichi
PY - 2010/6
Y1 - 2010/6
N2 - 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.
AB - 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.
KW - Alzheimer's disease
KW - Amyloid beta
KW - Catechol derivatives
KW - Fibril formation
KW - Inhibitor
KW - Liposome
UR - http://www.scopus.com/inward/record.url?scp=77952107424&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77952107424&partnerID=8YFLogxK
U2 - 10.1016/j.jbiosc.2009.11.010
DO - 10.1016/j.jbiosc.2009.11.010
M3 - Article
C2 - 20471605
AN - SCOPUS:77952107424
VL - 109
SP - 629
EP - 634
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
SN - 1389-1723
IS - 6
ER -