Effect of liposome membranes on disaggregation of amyloid β fibrils by dopamine

Huong Thi Vu, Toshinori Shimanouchi, Daisuke Ishikawa, Tadaharu Matsumoto, Hisashi Yagi, Yuji Goto, Hiroshi Umakoshi, Ryoichi Kuboi

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The inhibition of fibril formation of amyloid β (Aβ) and the disaggregation of Aβ fibrils are the promising approaches for a medical treatment of Alzheimer's disease (AD) therapy. In this study, we investigated the effects of liposomes on dopamine-induced disaggregation of Aβ fibrils by using the variety of liposomes. The used liposomes were normal liposomes, raft-forming liposomes, charged liposomes and oxidized liposomes. Those liposome could accelerate the disaggregation rate of fibrils. From the comparison of normal and charged liposomes, a certain contribution of dopamine via an electrostatic interaction to the disaggregation was confirmed. From raft-forming and oxidized liposomes, we revealed a significant contribution of bound water to liposomes, which could assist the formation of the quinine-form of dopamine by a removal of its proton. It is, therefore, concluded that the membrane surface of liposomes is considered to be an adequate environment for the dopamine-induced disaggregation of fibrils.

Original languageEnglish
Pages (from-to)118-126
Number of pages9
JournalBiochemical Engineering Journal
Volume71
DOIs
Publication statusPublished - Feb 5 2013
Externally publishedYes

Fingerprint

Liposomes
Amyloid
Dopamine
Membranes
Quinine
Coulomb interactions
Static Electricity
Protons
Alzheimer Disease

Keywords

  • Alzheimer's disease
  • Amyloid beta fibrils
  • Catecholamines
  • Disaggregation
  • Liposome

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biomedical Engineering
  • Environmental Engineering

Cite this

Effect of liposome membranes on disaggregation of amyloid β fibrils by dopamine. / Vu, Huong Thi; Shimanouchi, Toshinori; Ishikawa, Daisuke; Matsumoto, Tadaharu; Yagi, Hisashi; Goto, Yuji; Umakoshi, Hiroshi; Kuboi, Ryoichi.

In: Biochemical Engineering Journal, Vol. 71, 05.02.2013, p. 118-126.

Research output: Contribution to journalArticle

Vu, Huong Thi ; Shimanouchi, Toshinori ; Ishikawa, Daisuke ; Matsumoto, Tadaharu ; Yagi, Hisashi ; Goto, Yuji ; Umakoshi, Hiroshi ; Kuboi, Ryoichi. / Effect of liposome membranes on disaggregation of amyloid β fibrils by dopamine. In: Biochemical Engineering Journal. 2013 ; Vol. 71. pp. 118-126.
@article{41f503c3caf74ed78166bf2f0a6faf1d,
title = "Effect of liposome membranes on disaggregation of amyloid β fibrils by dopamine",
abstract = "The inhibition of fibril formation of amyloid β (Aβ) and the disaggregation of Aβ fibrils are the promising approaches for a medical treatment of Alzheimer's disease (AD) therapy. In this study, we investigated the effects of liposomes on dopamine-induced disaggregation of Aβ fibrils by using the variety of liposomes. The used liposomes were normal liposomes, raft-forming liposomes, charged liposomes and oxidized liposomes. Those liposome could accelerate the disaggregation rate of fibrils. From the comparison of normal and charged liposomes, a certain contribution of dopamine via an electrostatic interaction to the disaggregation was confirmed. From raft-forming and oxidized liposomes, we revealed a significant contribution of bound water to liposomes, which could assist the formation of the quinine-form of dopamine by a removal of its proton. It is, therefore, concluded that the membrane surface of liposomes is considered to be an adequate environment for the dopamine-induced disaggregation of fibrils.",
keywords = "Alzheimer's disease, Amyloid beta fibrils, Catecholamines, Disaggregation, Liposome",
author = "Vu, {Huong Thi} and Toshinori Shimanouchi and Daisuke Ishikawa and Tadaharu Matsumoto and Hisashi Yagi and Yuji Goto and Hiroshi Umakoshi and Ryoichi Kuboi",
year = "2013",
month = "2",
day = "5",
doi = "10.1016/j.bej.2012.12.012",
language = "English",
volume = "71",
pages = "118--126",
journal = "Biochemical Engineering Journal",
issn = "1369-703X",
publisher = "Elsevier",

}

TY - JOUR

T1 - Effect of liposome membranes on disaggregation of amyloid β fibrils by dopamine

AU - Vu, Huong Thi

AU - Shimanouchi, Toshinori

AU - Ishikawa, Daisuke

AU - Matsumoto, Tadaharu

AU - Yagi, Hisashi

AU - Goto, Yuji

AU - Umakoshi, Hiroshi

AU - Kuboi, Ryoichi

PY - 2013/2/5

Y1 - 2013/2/5

N2 - The inhibition of fibril formation of amyloid β (Aβ) and the disaggregation of Aβ fibrils are the promising approaches for a medical treatment of Alzheimer's disease (AD) therapy. In this study, we investigated the effects of liposomes on dopamine-induced disaggregation of Aβ fibrils by using the variety of liposomes. The used liposomes were normal liposomes, raft-forming liposomes, charged liposomes and oxidized liposomes. Those liposome could accelerate the disaggregation rate of fibrils. From the comparison of normal and charged liposomes, a certain contribution of dopamine via an electrostatic interaction to the disaggregation was confirmed. From raft-forming and oxidized liposomes, we revealed a significant contribution of bound water to liposomes, which could assist the formation of the quinine-form of dopamine by a removal of its proton. It is, therefore, concluded that the membrane surface of liposomes is considered to be an adequate environment for the dopamine-induced disaggregation of fibrils.

AB - The inhibition of fibril formation of amyloid β (Aβ) and the disaggregation of Aβ fibrils are the promising approaches for a medical treatment of Alzheimer's disease (AD) therapy. In this study, we investigated the effects of liposomes on dopamine-induced disaggregation of Aβ fibrils by using the variety of liposomes. The used liposomes were normal liposomes, raft-forming liposomes, charged liposomes and oxidized liposomes. Those liposome could accelerate the disaggregation rate of fibrils. From the comparison of normal and charged liposomes, a certain contribution of dopamine via an electrostatic interaction to the disaggregation was confirmed. From raft-forming and oxidized liposomes, we revealed a significant contribution of bound water to liposomes, which could assist the formation of the quinine-form of dopamine by a removal of its proton. It is, therefore, concluded that the membrane surface of liposomes is considered to be an adequate environment for the dopamine-induced disaggregation of fibrils.

KW - Alzheimer's disease

KW - Amyloid beta fibrils

KW - Catecholamines

KW - Disaggregation

KW - Liposome

UR - http://www.scopus.com/inward/record.url?scp=84872035920&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84872035920&partnerID=8YFLogxK

U2 - 10.1016/j.bej.2012.12.012

DO - 10.1016/j.bej.2012.12.012

M3 - Article

AN - SCOPUS:84872035920

VL - 71

SP - 118

EP - 126

JO - Biochemical Engineering Journal

JF - Biochemical Engineering Journal

SN - 1369-703X

ER -