Evidence map›Paper›PMID 33979140›Full record

ArticleACS chemical neuroscience2021

Natural Compound from Olive Oil Inhibits S100A9 Amyloid Formation and Cytotoxicity: Implications for Preventing Alzheimer's Disease.

Manuela Leri, Himanshu Chaudhary, Igor A Iashchishyn, Jonathan Pansieri, Željko M Svedružić, Silvia Gómez Alcalde, Greta Musteikyte, Vytautas Smirnovas, Massimo Stefani, Monica Bucciantini and 1 more

Open access · hybridAbstract read
In one paragraph

Article in ACS chemical neuroscience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
3.0field-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

13 citing papers in PubMed, 1 synthesis or guideline pooled it, 31 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

11 authors at 4 institutions in 4 countries.

Manuela LeriDepartment of Experimental and Clinical Biomedical Sciences "Mario Serio", University of Florence, 50134 Florence, Italy.
Himanshu ChaudharyDepartment of Medical Biochemistry and Biophysics, Umeå University, 90187 Umeå, Sweden.
Igor A IashchishynDepartment of Medical Biochemistry and Biophysics, Umeå University, 90187 Umeå, Sweden.ORCID 0000-0002-1691-9025
Jonathan PansieriDepartment of Medical Biochemistry and Biophysics, Umeå University, 90187 Umeå, Sweden.ORCID 0000-0001-8918-9943
Željko M SvedružićDepartment of Biotechnology, University of Rijeka, HR 51000 Rijeka, Croatia.ORCID 0000-0002-0736-6182
Silvia Gómez AlcaldeDepartment of Medical Biochemistry and Biophysics, Umeå University, 90187 Umeå, Sweden.
Greta MusteikyteInstitute of Biotechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, Lithuania.
Vytautas SmirnovasInstitute of Biotechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, Lithuania.
Massimo StefaniDepartment of Experimental and Clinical Biomedical Sciences "Mario Serio", University of Florence, 50134 Florence, Italy.
Monica BucciantiniDepartment of Experimental and Clinical Biomedical Sciences "Mario Serio", University of Florence, 50134 Florence, Italy.
Ludmilla A Morozova-RocheDepartment of Medical Biochemistry and Biophysics, Umeå University, 90187 Umeå, Sweden.ORCID 0000-0001-5886-2023
Umeå University · SEUniversity of Florence · ITVilnius University · LTUniversity of Rijeka · HR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polyphenolic compounds in the Mediterranean diet have received increasing attention due to their protective properties in amyloid neurodegenerative and many other diseases. Here, we have demonstrated for the first time that polyphenol oleuropein aglycone (OleA), which is the most abundant compound in olive oil, has multiple potencies for the inhibition of amyloid self-assembly of pro-inflammatory protein S100A9 and the mitigation of the damaging effect of its amyloids on neuroblastoma SH-SY5Y cells. OleA directly interacts with both native and fibrillar S100A9 as shown by intrinsic fluorescence and molecular dynamic simulation. OleA prevents S100A9 amyloid oligomerization as shown using amyloid oligomer-specific antibodies and cross-β-sheet formation detected by circular dichroism. It decreases the length of amyloid fibrils measured by atomic force microscopy (AFM) as well as reduces the effective rate of amyloid growth and the overall amyloid load as derived from the kinetic analysis of amyloid formation. OleA disintegrates already preformed fibrils of S100A9, converting them into nonfibrillar and nontoxic aggregates as revealed by amyloid thioflavin-T dye binding, AFM, and cytotoxicity assays. At the cellular level, OleA targets S100A9 amyloids already at the membranes as shown by immunofluorescence and fluorescence resonance energy transfer, significantly reducing the amyloid accumulation in GM1 ganglioside containing membrane rafts. OleA increases overall cell viability when neuroblastoma cells are subjected to the amyloid load and alleviates amyloid-induced intracellular rise of reactive oxidative species and free Ca

Indexed as

Alzheimer DiseaseAmyloidAmyloid beta-PeptidesAmyloidogenic ProteinsHumansKineticsOlive OilAmyloidAmyloid beta-PeptidesAmyloidogenic ProteinsOlive Oilamyloidcytotoxicityneurodegenerationoleuropein aglyconeplant polyphenolsS100A9

Identifiers

PMID33979140
PMCPMC8291483
OpenAlexW3162869726

What OpenQuestion holds

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LicenceCC BY
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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.