Evidence map›Paper›PMID 31702868›Full record

ArticleChembiochem : a European journal of chemical biology2020

Real-Time BODIPY-Binding Assay To Screen Inhibitors of the Early Oligomerization Process of Aβ1-42 Peptide.

Nicolo Tonali, Veronica I Dodero, Julia Kaffy, Loreen Hericks, Sandrine Ongeri, Norbert Sewald

Open access · hybridAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

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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

6 authors at 2 institutions in 2 countries.

Nicolo TonaliOrganic and Bioorganic Chemistry, Department of Chemistry, Bielefeld University, P. O. Box 100131, 33501, Bielefeld, Germany.ORCID 0000-0002-1435-5676
Veronica I DoderoOrganic and Bioorganic Chemistry, Department of Chemistry, Bielefeld University, P. O. Box 100131, 33501, Bielefeld, Germany.ORCID 0000-0001-7937-1880
Julia KaffyBioCIS, CNRS/Université Paris Sud, Université Paris Saclay, 5 rue Jean-Baptiste Clément, 92296, Châtenay-Malabry Cedex, France.ORCID 0000-0002-1725-9268
Loreen HericksOrganic and Bioorganic Chemistry, Department of Chemistry, Bielefeld University, P. O. Box 100131, 33501, Bielefeld, Germany.
Sandrine OngeriBioCIS, CNRS/Université Paris Sud, Université Paris Saclay, 5 rue Jean-Baptiste Clément, 92296, Châtenay-Malabry Cedex, France.ORCID 0000-0002-2118-7324
Norbert SewaldOrganic and Bioorganic Chemistry, Department of Chemistry, Bielefeld University, P. O. Box 100131, 33501, Bielefeld, Germany.ORCID 0000-0002-0309-2655
Bielefeld University · DEUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Misfolding and aggregation of amyloid β1-42 peptide (Aβ1-42) play a central role in the pathogenesis of Alzheimer's disease (AD). Targeting the highly cytotoxic oligomeric species formed during the early stages of the aggregation process represents a promising therapeutic strategy to reduce the toxicity associated with Aβ1-42. Currently, the thioflavin T (ThT) assay is the only established spectrofluorometric method to screen aggregation inhibitors. The success of the ThT assay is that it can detect Aβ1-42 aggregates with high β-sheet content, such as protofibrils or fibrils, which appear in the late aggregation steps. Unfortunately, by using the ThT assay, the detection of inhibitors of early soluble oligomers that present a low β-sheet character is challenging. Herein, a new, facile, and robust boron-dipyrromethene (BODIPY) real-time assay suitable for 96-well plate format, which allows screening of compounds as selective inhibitors of the formation of Aβ1-42 oligomers, is reported. These inhibitors decrease the cellular toxicity of Aβ1-42, although they fail in the ThT assay. The findings have been confirmed and validated by structural analysis and cell viability assays under comparable experimental conditions. It is demonstrated that the BODIPY assay is a convenient method to screen and discover new candidate compounds that slow down or stop the pathological early oligomerization process and are active in the cellular assay. Therefore, it is a suitable complementary screening method of the current ThT assay.

Indexed as

Amyloid beta-PeptidesBoron CompoundsDrug MonitoringHigh-Throughput Screening AssaysHumansNeuroprotective AgentsPeptide FragmentsSmall Molecule Libraries4,4-difluoro-4-bora-3a,4a-diaza-s-indaceneAmyloid beta-Peptidesamyloid beta-protein (1-42)Boron CompoundsNeuroprotective AgentsPeptide FragmentsSmall Molecule LibrariesAlzheimer's diseaseamyloid beta-peptidesfluorescenceinhibitorsoligomerization

Identifiers

PMID31702868
PMCPMC7217026
OpenAlexW2984890825

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.