Evidence map›Paper›PMID 35745206›Full record

ArticleNutrients2022

Hydroxybenzoic Acids as Acetylcholinesterase Inhibitors: Calorimetric and Docking Simulation Studies.

Grażyna Budryn, Iwona Majak, Joanna Grzelczyk, Dominik Szwajgier, Alejandro Rodríguez-Martínez, Horacio Pérez-Sánchez

Open access · goldAbstract read
In one paragraph

Article in Nutrients, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

24 citing papers in PubMed, 41 citations in OpenAlex.

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  9. Bioactive Potential and Chemical Composition ofMolecules (Basel, Switzerland) · 2025
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  10. α-Glucosidase, butyrylcholinesterase and acetylcholinesterase inhibitory activities of phenolic compounds fromSaudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2024
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  13. Current issues in molecular biology · 2023
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  18. International journal of molecular sciences · 2023
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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 3 institutions in 2 countries.

Grażyna BudrynInstitute of Food Technology and Analysis, Faculty of Biotechnology and Food Sciences, Lodz University of Technology, Stefanowskiego 2/22, 90-537 Lodz, Poland.ORCID 0000-0002-8050-3702
Iwona MajakInstitute of Food Technology and Analysis, Faculty of Biotechnology and Food Sciences, Lodz University of Technology, Stefanowskiego 2/22, 90-537 Lodz, Poland.
Joanna GrzelczykInstitute of Food Technology and Analysis, Faculty of Biotechnology and Food Sciences, Lodz University of Technology, Stefanowskiego 2/22, 90-537 Lodz, Poland.ORCID 0000-0002-0802-7115
Dominik SzwajgierDepartment of Biotechnology, Microbiology and Human Nutrition, University of Life Sciences in Lublin, Skromna 8, 20-704 Lublin, Poland.ORCID 0000-0002-2285-0669
Alejandro Rodríguez-MartínezStructural Bioinformatics and High-Performance Computing Research Group (BIO-HPC), Computer Engineering Department, Universidad Católica de Murcia (UCAM), Guadalupe, 30107 Murcia, Spain.
Horacio Pérez-SánchezStructural Bioinformatics and High-Performance Computing Research Group (BIO-HPC), Computer Engineering Department, Universidad Católica de Murcia (UCAM), Guadalupe, 30107 Murcia, Spain.ORCID 0000-0003-4468-7898
Lodz University of Technology · PLUniversidad Católica de Murcia · ESUniversity of Life Sciences in Lublin · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One of the symptoms of Alzheimer's disease (AD) is low acetylcholine level due to high acetylcholinesterase (AChE) activity. For this reason, AChE inhibitors are used in the treatment of AD, the prolonged use of which may cause a cholinergic crisis. There is a need to search for safe natural AChE inhibitors. The study analyzed 16 hydroxybenzoic acids using calorimetry and docking simulation as AChE inhibitors. All tested compounds were shown to inhibit the hydrolysis of ACh. The best properties were shown by methyl syringinate, which acted as competitive inhibitor at a catalytic site. The tested compounds also interacted with the anionic or peripheral binding site known to block β-amyloid plaques formation. The activity of the tested hydroxybenzoic acids IC50 ranged from 5.50 to 34.19 µmol/µmol of AChE, and the binding constant Ka from 20.53 to 253.16 L/mol, which proves their reversible, non-toxic effect, and activity at physiological concentrations.

Indexed as

Alzheimer DiseaseCholinesterase InhibitorsAcetylcholineAcetylcholinesteraseCalorimetryHumansHydroxybenzoatesMolecular Docking SimulationAcetylcholineAcetylcholinesteraseCholinesterase InhibitorsHydroxybenzoatesacetylcholinesteraseAlzheimer diseasedocking simulationhydroxybenzoic acidsITC

Identifiers

PMID35745206
PMCPMC9227119
OpenAlexW4283021333

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.