Evidence map›Paper›PMID 35055076›Full record

ArticleInternational journal of molecular sciences2022

The Effect of Ethanol on Disassembly of Amyloid-β

Atsuya Matsui, Jean-Pierre Bellier, Takeshi Kanai, Hiroki Satooka, Akio Nakanishi, Tsukasa Terada, Takafumi Ishibe, Yoshiaki Nakamura, Hiroyasu Taguchi, Nobuyasu Naruse and 1 more

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Article
  2. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors.

Atsuya MatsuiDepartment of Fundamental Bioscience, Shiga University of Medical Science, Otsu 520-2192, Japan.
Jean-Pierre BellierMolecular Neuroscience Research Center, Shiga University of Medical Science, Otsu 520-2192, Japan.ORCID 0000-0002-8758-8075
Takeshi KanaiDepartment of Fundamental Bioscience, Shiga University of Medical Science, Otsu 520-2192, Japan.
Hiroki SatookaDepartment of Fundamental Bioscience, Shiga University of Medical Science, Otsu 520-2192, Japan.
Akio NakanishiDepartment of Fundamental Bioscience, Shiga University of Medical Science, Otsu 520-2192, Japan.
Tsukasa TeradaGraduate School of Engineering Science, Osaka University, 1-3 Machikaneyama-Cho, Toyonaka 560-8531, Japan.
Takafumi IshibeGraduate School of Engineering Science, Osaka University, 1-3 Machikaneyama-Cho, Toyonaka 560-8531, Japan.
Yoshiaki NakamuraGraduate School of Engineering Science, Osaka University, 1-3 Machikaneyama-Cho, Toyonaka 560-8531, Japan.
Hiroyasu TaguchiMolecular Neuroscience Research Center, Shiga University of Medical Science, Otsu 520-2192, Japan.
Nobuyasu NaruseDepartment of Fundamental Bioscience, Shiga University of Medical Science, Otsu 520-2192, Japan.ORCID 0000-0003-3934-2641
Yutaka MeraDepartment of Fundamental Bioscience, Shiga University of Medical Science, Otsu 520-2192, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Amyloid beta-PeptidesElectrophoresisEthanolHumansMicroscopy, Atomic ForcePeptide FragmentsProtein AggregatesProtein Aggregation, PathologicalProtein MultimerizationAmyloid beta-Peptidesamyloid beta-protein (1-42)EthanolPeptide FragmentsProtein Aggregatesamyloid-βatomic force microscopyGaussian fittinggel electrophoresisoligomer

Identifiers

PMID35055076
PMCPMC8779648

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.