Evidence map›Paper›PMID 33375009›Full record

ArticleInternational journal of molecular sciences2020

Effect of Amyloid-β Monomers on Lipid Membrane Mechanical Parameters-Potential Implications for Mechanically Driven Neurodegeneration in Alzheimer's Disease.

Dominik Drabik, Grzegorz Chodaczek, Sebastian Kraszewski

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.2field-weighted citation impact, top 22% of its field
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

11 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Specific Binding of Alzheimer's Aβ Peptides to Extracellular Vesicles.International journal of molecular sciences · 2024
    Article
  5. Review
  6. Membrane Proteins: Structure, Function and Motion.International journal of molecular sciences · 2022
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Interactions of Amyloid-β with Membrane Proteins.International journal of molecular sciences · 2021
    Review
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

3 authors at 3 institutions in 1 country.

Dominik DrabikLaboratory of Cytobiochemistry, Faculty of Biotechnology, University of Wrocław, F. Joliot-Curie 14a, 50-383 Wrocław, Poland.ORCID 0000-0003-4568-4066
Grzegorz ChodaczekŁukasiewicz Research Network-PORT Polish Center for Technology Development, Stabłowicka 147, 54-066 Wrocław, Poland.
Sebastian KraszewskiDepartment of Biomedical Engineering, Faculty of Fundamental Problems of Technology, Wrocław University of Science and Technology, Pl. Grunwaldzki 13, 50-377 Wrocław, Poland.ORCID 0000-0003-3244-7694
Łukasiewicz Research Network – PORT Polish Center for Technology Development · PLUniversity of Wrocław · PLWrocław University of Science and Technology · PL

Funding

National Science Centre 2016/21/N/NZ1/02767National Science Centre 2018/30/E/NZ1/00099
6 · The paper itself

Abstract

Alzheimer's disease (AD) is a neurodegenerative disease that results in memory loss and the impairment of cognitive skills. Several mechanisms of AD's pathogenesis were proposed, such as the progressive accumulation of amyloid-β (Aβ) and τ pathology. Nevertheless, the exact neurodegenerative mechanism of the Aβ remains complex and not fully understood. This paper proposes an alternative hypothesis of the mechanism based on maintaining the neuron membrane's mechanical balance. The incorporation of Aβ decreases the lipid membrane's elastic properties, which eventually leads to the impairment of membrane clustering, disruption of mechanical wave propagation, and change in gamma oscillations. The first two disrupt the neuron's ability to function correctly while the last one decreases sensory encoding and perception enabling. To begin discussing this mechanical-balance hypothesis, we measured the effect of two selected peptides, Aβ-40 and Aβ-42, as well as their fluorescently labeled modification, on membrane mechanical properties. The decrease of bending rigidity, consistent for all investigated peptides, was observed using molecular dynamic studies and experimental flicker-noise techniques. Additionally, wave propagation was investigated with molecular dynamic studies in membranes with and without incorporated neurodegenerative peptides. A change in membrane behavior was observed in the membrane system with incorporated Aβ.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesBrainCell MembraneHumansLipid BilayersMembrane LipidsMembrane PotentialsMicroscopy, ConfocalMolecular Dynamics SimulationNeurodegenerative DiseasesNeuronsPeptide FragmentsPhosphatidylcholines1-palmitoyl-2-oleoylphosphatidylcholineAmyloid beta-Peptidesamyloid beta-protein (1-40)amyloid beta-protein (1-42)Lipid BilayersMembrane LipidsPeptide FragmentsPhosphatidylcholinesamyloid-beta peptidesflicker-noise spectroscopygiant unilamellar vesiclesmembrane mechanicsmolecular dynamicsneurodegenerationpressure wave

Identifiers

PMID33375009
PMCPMC7792773
OpenAlexW3114793173

What OpenQuestion holds

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Registered trials

None linked

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.