Evidence map›Paper›PMID 32942739›Full record

ArticleBiomolecules2020

Curcumin Inhibits the Primary Nucleation of Amyloid-Beta Peptide: A Molecular Dynamics Study.

Irini Doytchinova, Mariyana Atanasova, Evdokiya Salamanova, Stefan Ivanov, Ivan Dimitrov

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

25 citing papers in PubMed, 65 citations in OpenAlex.

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  20. Benefits of dietary polyphenols in Alzheimer's disease.Frontiers in aging neuroscience · 2022
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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

5 authors at 2 institutions in 2 countries.

Irini DoytchinovaFaculty of Pharmacy, Medical University of Sofia, 2 Dunav st., 1000 Sofia, Bulgaria.ORCID 0000-0002-1469-1768
Mariyana AtanasovaFaculty of Pharmacy, Medical University of Sofia, 2 Dunav st., 1000 Sofia, Bulgaria.
Evdokiya SalamanovaFaculty of Pharmacy, Medical University of Sofia, 2 Dunav st., 1000 Sofia, Bulgaria.
Stefan IvanovFaculty of Pharmacy, Medical University of Sofia, 2 Dunav st., 1000 Sofia, Bulgaria.ORCID 0000-0002-6949-2328
Ivan DimitrovFaculty of Pharmacy, Medical University of Sofia, 2 Dunav st., 1000 Sofia, Bulgaria.ORCID 0000-0003-4838-312X
Medical University of Sofia · BGUniversity of Maryland, Baltimore · US

Funding

Bulgarian National Science Fund DN03/9/2016Medical Science Council of the Medical University of Sofia D-118/2020Science and Education for Smart Growth BG05M2OP001-1.001-0003
6 · The paper itself

Abstract

The amyloid plaques are a key hallmark of neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease. Amyloidogenesis is a complex long-lasting multiphase process starting with the formation of nuclei of amyloid peptides: a process assigned as a primary nucleation. Curcumin (CU) is a well-known inhibitor of the aggregation of amyloid-beta (Aβ) peptides. Even more, CU is able to disintegrate preformed Aβ firbils and amyloid plaques. Here, we simulate by molecular dynamics the primary nucleation process of 12 Aβ peptides and investigate the effects of CU on the process. We found that CU molecules intercalate among the Aβ chains and bind tightly to them by hydrogen bonds, hydrophobic, π-π, and cation-π interactions. In the presence of CU, the Aβ peptides form a primary nucleus of a bigger size. The peptide chains in the nucleus become less flexible and more disordered, and the number of non-native contacts and hydrogen bonds between them decreases. For comparison, the effects of the weaker Aβ inhibitor ferulic acid (FA) on the primary nucleation are also examined. Our study is in good agreement with the observation that taken regularly, CU is able to prevent or at least delay the onset of neurodegenerative disorders.

Indexed as

Alzheimer DiseaseAmyloidAmyloid beta-PeptidesBinding SitesCoumaric AcidsCurcuminHumansHydrogen BondingHydrophobic and Hydrophilic InteractionsMolecular Dynamics SimulationNeuroprotective AgentsProtein AggregatesProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsAmyloidAmyloid beta-PeptidesCoumaric AcidsCurcuminferulic acidNeuroprotective AgentsProtein Aggregatesamyloid-beta peptidecurcuminferulic acidmolecular dynamics

Identifiers

PMID32942739
PMCPMC7563689
OpenAlexW3084975119

What OpenQuestion holds

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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.