Evidence map›Paper›PMID 26880066›Full record

ArticleScientific reports2016

Amyloid-β peptides in interaction with raft-mime model membranes: a neutron reflectivity insight.

Valeria Rondelli, Paola Brocca, Simona Motta, Massimo Messa, Laura Colombo, Mario Salmona, Giovanna Fragneto, Laura Cantù, Elena Del Favero

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

14 citing papers in PubMed, 32 citations in OpenAlex.

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  13. Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes.Proceedings of the National Academy of Sciences of the United States of America · 2017
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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

9 authors at 4 institutions in 2 countries.

Valeria RondelliDept. of Medical Biotechnologies and Traslational Medicine, University of Milano, LITA, Via F.lli Cervi, 93. 20090 Segrate (Milano), Italy.
Paola BroccaDept. of Medical Biotechnologies and Traslational Medicine, University of Milano, LITA, Via F.lli Cervi, 93. 20090 Segrate (Milano), Italy.
Simona MottaDept. of Medical Biotechnologies and Traslational Medicine, University of Milano, LITA, Via F.lli Cervi, 93. 20090 Segrate (Milano), Italy.
Massimo MessaDept. of Molecular Biochemistry and Pharmacology, IRCCS Istituto di Ricerche Farmacologiche "Mario Negri", Via La Masa 19, 20156 Milan, Italy.
Laura ColomboDept. of Molecular Biochemistry and Pharmacology, IRCCS Istituto di Ricerche Farmacologiche "Mario Negri", Via La Masa 19, 20156 Milan, Italy.
Mario SalmonaDept. of Molecular Biochemistry and Pharmacology, IRCCS Istituto di Ricerche Farmacologiche "Mario Negri", Via La Masa 19, 20156 Milan, Italy.
Giovanna FragnetoInstitut Laue-Langevin, 71 avenue des Martyrs, BP 156, 38000 Grenoble Cedex, France.
Laura CantùDept. of Medical Biotechnologies and Traslational Medicine, University of Milano, LITA, Via F.lli Cervi, 93. 20090 Segrate (Milano), Italy.
Elena Del FaveroDept. of Medical Biotechnologies and Traslational Medicine, University of Milano, LITA, Via F.lli Cervi, 93. 20090 Segrate (Milano), Italy.
University of Milan · ITIstituti di Ricovero e Cura a Carattere Scientifico · ITInstitut Laue-Langevin · FRMario Negri Institute for Pharmacological Research · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The role of first-stage β-amyloid aggregation in the development of the Alzheimer disease, is widely accepted but still unclear. Intimate interaction with the cell membrane is invoked. We designed Neutron Reflectometry experiments to reveal the existence and extent of the interaction between β-amyloid (Aβ) peptides and a lone customized biomimetic membrane, and their dependence on the aggregation state of the peptide. The membrane, asymmetrically containing phospholipids, GM1 and cholesterol in biosimilar proportion, is a model for a raft, a putative site for amyloid-cell membrane interaction. We found that the structured-oligomer of Aβ(1-42), its most acknowledged membrane-active state, is embedded as such into the external leaflet of the membrane. Conversely, the Aβ(1-42) unstructured early-oligomers deeply penetrate the membrane, likely mimicking the interaction at neuronal cell surfaces, when the Aβ(1-42) is cleaved from APP protein and the membrane constitutes a template for its further structural evolution. Moreover, the smaller Aβ(1-6) fragment, the N-terminal portion of Aβ, was also used. Aβ N-terminal is usually considered as involved in oligomer stabilization but not in the peptide-membrane interaction. Instead, it was seen to remove lipids from the bilayer, thus suggesting its role, once in the whole peptide, in membrane leakage, favouring peptide recruitment.

Indexed as

Biological MimicryLipid BilayersAlzheimer DiseaseAmyloid beta-PeptidesBiomimeticsCell MembraneGangliosidosis, GM1HumansNeutronsProtein BindingProtein MultimerizationAmyloid beta-PeptidesLipid Bilayers

Identifiers

PMID26880066
PMCPMC4754687
OpenAlexW2410135302

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.