@article{oai:shiga-med.repo.nii.ac.jp:00004094,
 author = {松井, 温哉 and 金井, 岳志 and 里岡, 大樹 and 中西, 章夫 and 田口, 弘康 and 成瀬, 延康 and 目良, 裕 and MATSUI, Atsuya and BELLIER, Jean-Pierre and KANAI, Takeshi and SATOOKA, Hiroki and NAKANISHI, Akio and TERADA, Tsukasa and ISHIBE, Takafumi and NAKAMURA, Yoshiaki and TAGUCHI, Hiroyasu and NARUSE, Nobuyasu and MERA, Yutaka},
 issue = {2},
 journal = {International journal of molecular sciences},
 month = {Jan},
 note = {pdf, The most common type of dementia, Alzheimer's disease, is associated with senile plaques formed by the filamentous aggregation of hydrophobic amyloid-β (Aβ) in the brains of patients. Small oligomeric assemblies also occur and drugs and chemical compounds that can interact with such assemblies have attracted much attention. However, these compounds need to be solubilized in appropriate solvents, such as ethanol, which may also destabilize their protein structures. As the impact of ethanol on oligomeric Aβ assembly is unknown, we investigated the effect of various concentrations of ethanol (0 to 7.2 M) on Aβ pentameric assemblies (Aβp) by combining blue native-PAGE (BN-PAGE) and ambient air atomic force microscopy (AFM). This approach was proven to be very convenient and reliable for the quantitative analysis of Aβ assembly. The Gaussian analysis of the height histogram obtained from the AFM images was correlated with band intensity on BN-PAGE for the quantitative estimation of Aβp. Our observations indicated up to 1.4 M (8.3%) of added ethanol can be used as a solvent/vehicle without quantitatively affecting Aβ pentamer stability. Higher concentration induced significant destabilization of Aβp and eventually resulted in the complete disassembly of Aβp., Journal Article},
 title = {The Effect of Ethanol on Disassembly of Amyloid-β1-42 Pentamer Revealed by Atomic Force Microscopy and Gel Electrophoresis.},
 volume = {23},
 year = {2022}
}