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
N1 - Funding Information:
The fundamental concept of this study was supported by the Research Group of “Membrane Stress Biotechnology”. It was partly funded by a Grant-in-Aid for Scientific Research (Nos. 21246121, 23656525, and 24606086 ) from the Ministry of Education, Science, Sports, and Culture of Japan and a Cabinet Office, Government of Japan through its “Funding Program for Next Generation World-Leading Researchers” (No. GR066 ). The authors are grateful to the Research Center for Solar Energy Chemistry of Osaka University and the Gas hydrate Analyzing System of Osaka University. The TEM images were taken at the Research Center for Ultrahigh Voltage Electron Microscopy, Osaka University, Japan.
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
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U2 - 10.1016/j.bej.2012.12.012
DO - 10.1016/j.bej.2012.12.012
M3 - Article
AN - SCOPUS:84872035920
SN - 1369-703X
VL - 71
SP - 118
EP - 126
JO - Biochemical Engineering Journal
JF - Biochemical Engineering Journal
ER -