Evidence map›Paper›PMID 32499589›Full record

ArticleScientific reports2020

Amyloid Aggregation of Insulin: An Interaction Study of Green Tea Constituents.

Miroslav Gancar, Elena Kurin, Zuzana Bednarikova, Jozef Marek, Pavel Mucaji, Milan Nagy, Zuzana Gazova

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 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
4.5field-weighted citation impact, top 4% 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, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. The influence of cations on α-lactalbumin amyloid aggregation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Article
  7. Review
  8. Article
  9. Polyphenol-solubility alters amyloid fibril formation of α-synuclein.Protein science : a publication of the Protein Society · 2021
    Article
  10. Review
  11. Article
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

7 authors at 3 institutions in 1 country.

Miroslav GancarDepartment of Biophysics, Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 040 01, Kosice, Slovakia.
Elena KurinDepartment of Pharmacognosy and Botany, Faculty of Pharmacy, Comenius University in Bratislava, Odbojarov 10, 832 32, Bratislava, Slovakia. elena.kurin@uniba.sk.
Zuzana BednarikovaDepartment of Biophysics, Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 040 01, Kosice, Slovakia.
Jozef MarekDepartment of Biophysics, Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 040 01, Kosice, Slovakia.
Pavel MucajiDepartment of Pharmacognosy and Botany, Faculty of Pharmacy, Comenius University in Bratislava, Odbojarov 10, 832 32, Bratislava, Slovakia.
Milan NagyDepartment of Pharmacognosy and Botany, Faculty of Pharmacy, Comenius University in Bratislava, Odbojarov 10, 832 32, Bratislava, Slovakia.
Zuzana GazovaDepartment of Biophysics, Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 040 01, Kosice, Slovakia. gazova@saske.sk.
Comenius University Bratislava · SKInstitute of Experimental Physics of the Slovak Academy of Sciences · SKSlovak Academy of Sciences · SK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Exogenous insulin, used as a therapeutic agent for diabetes, forms insoluble deposits containing amyloid fibrillar structures near the administration site. We have analyzed the in vitro anti-amyloid activity of four green tea constituents: (-)-epigallocatechin gallate (EGCG), (-)-epicatechin (EC), gallic acid (GA), caffeine (CF), and their equimolar mixtures. Regarding individually tested compounds, only EGCG inhibited the fibrillization process. The individual EC, GA, and CF molecules were ineffective. The presence of EGCG in equimolar combinations with GA, EC, or CF was required for the inhibitory activity of most mixtures. Molecular docking revealed that EGCG interacts with an essential amyloidogenic region of insulin chain B. Individually inactive GA had a potentiating effect on the activity of EGCG. In contrast, EC and CF had a negative impact on the activity of the mixtures. We have observed diverse morphology and the amount of insulin amyloid aggregates formed in the presence of studied compounds. The distinct types of amyloid aggregates created in vitro in the presence of EGCG and other green tea constituents were characterized. Results indicate that the biological activity of individual molecules is not directly applicable to the pooled samples effects prediction.

Indexed as

AmyloidBinding SitesCaffeineCatechinGallic AcidHumansInsulinKineticsMolecular Docking SimulationProtein AggregatesProtein Structure, SecondaryTeaAmyloidCaffeineCatechinepigallocatechin gallateGallic AcidInsulinProtein AggregatesTea

Identifiers

PMID32499589
PMCPMC7272432
OpenAlexW3033153447

What OpenQuestion holds

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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.