Evidence map›Paper›PMID 37047766›Full record

ArticleInternational journal of molecular sciences2023

Molecular Docking and Dynamics Simulation Studies Predict Potential Anti-ADAR2 Inhibitors: Implications for the Treatment of Cancer, Neurological, Immunological and Infectious Diseases.

Emmanuel Broni, Andrew Striegel, Carolyn Ashley, Patrick O Sakyi, Saqib Peracha, Miriam Velazquez, Kristeen Bebla, Monsheel Sodhi, Samuel K Kwofie, Adesanya Ademokunwa and 2 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

10 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. ADAR Family Proteins: A Structural Review.Current issues in molecular biology · 2024
    Review
  5. Article
  6. Article
  7. Identifying potential monkeypox virus inhibitors: anFrontiers in cellular and infection microbiology · 2024
    Article
  8. Article
  9. Article
  10. 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

12 authors at 3 institutions in 2 countries.

Emmanuel BroniDepartment of Medicine, Loyola University Medical Center, Loyola University Chicago, Maywood, IL 60153, USA.ORCID 0000-0002-6793-7530
Andrew StriegelDepartment of Medicine, Loyola University Medical Center, Loyola University Chicago, Maywood, IL 60153, USA.
Carolyn AshleyDepartment of Medicine, Loyola University Medical Center, Loyola University Chicago, Maywood, IL 60153, USA.
Patrick O SakyiDepartment of Chemistry, School of Physical and Mathematical Sciences, College of Basic and Applied Sciences, University of Ghana, Legon, Accra P.O. Box LG 56, Ghana.
Saqib PerachaDepartment of Medicine, Loyola University Medical Center, Loyola University Chicago, Maywood, IL 60153, USA.
Miriam VelazquezDepartment of Medicine, Loyola University Medical Center, Loyola University Chicago, Maywood, IL 60153, USA.
Kristeen BeblaDepartment of Molecular Pharmacology & Neuroscience, Loyola University Medical Center, Loyola University Chicago, Maywood, IL 60153, USA.
Monsheel SodhiDepartment of Molecular Pharmacology & Neuroscience, Loyola University Medical Center, Loyola University Chicago, Maywood, IL 60153, USA.
Samuel K KwofieDepartment of Biomedical Engineering, School of Engineering Sciences, College of Basic & Applied Sciences, University of Ghana, Legon, Accra P.O. Box LG 77, Ghana.ORCID 0000-0002-1093-1517
Adesanya AdemokunwaDepartment of Medicine, Loyola University Medical Center, Loyola University Chicago, Maywood, IL 60153, USA.
Sufia KhanDepartment of Medicine, Loyola University Medical Center, Loyola University Chicago, Maywood, IL 60153, USA.
Whelton A MillerDepartment of Medicine, Loyola University Medical Center, Loyola University Chicago, Maywood, IL 60153, USA.ORCID 0000-0003-3822-7940
Loyola University Medical Center · USUniversity of Ghana · GHUniversity of Notre Dame · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Altered RNA editing has been linked to several neurodevelopmental disorders, including autism spectrum disorder (ASD) and intellectual disability, in addition to depression, schizophrenia, some cancers, viral infections and autoimmune disorders. The human ADAR2 is a potential therapeutic target for managing these various disorders due to its crucial role in adenosine to inosine editing. This study applied consensus scoring to rank potential ADAR2 inhibitors after performing molecular docking with AutoDock Vina and Glide (Maestro), using a library of 35,161 compounds obtained from traditional Chinese medicine. A total of 47 compounds were predicted to be good binders of the human ADAR2 and had insignificant toxicity concerns. Molecular dynamics (MD) simulations, including the molecular mechanics Poisson-Boltzmann surface area (MM/PBSA) procedure, also emphasized the binding of the shortlisted compounds. The potential compounds had plausible binding free energies ranging from -81.304 to -1068.26 kJ/mol from the MM/PBSA calculations. ZINC000085511995, a naphthoquinone had more negative binding free energy (-1068.26 kJ/mol) than inositol hexakisphosphate (IHP) [-873.873 kJ/mol], an agonist and a strong binder of ADAR2. The potential displacement of IHP by ZINC000085511995 in the IHP binding site of ADAR2 could be explored for possible deactivation of ADAR2. Bayesian-based biological activity prediction corroborates the neuropharmacological, antineoplastic and antiviral activity of the potential lead compounds. All the potential lead compounds, except ZINC000014612330 and ZINC000013462928, were predicted to be inhibitors of various deaminases. The potential lead compounds also had probability of activity (Pa) > 0.442 and probability of inactivity (Pi) < 0.116 values for treating acute neurologic disorders, except for ZINC000085996580 and ZINC000013462928. Pursuing these compounds for their anti-ADAR2 activities holds a promising future, especially against neurological disorders, some cancers and viral infections caused by RNA viruses. Molecular interaction, hydrogen bond and per-residue decomposition analyses predicted Arg400, Arg401, Lys519, Trp687, Glu689, and Lys690 as hot-spot residues in the ADAR2 IHP binding site. Most of the top compounds were observed to have naphthoquinone, indole, furanocoumarin or benzofuran moieties. Serotonin and tryptophan, which are beneficial in digestive regulation, improving sleep cycle and mood, are indole derivatives. These chemical series may have the potential to treat neurological disorders, prion diseases, some cancers, specific viral infections, metabolic disorders and eating disorders through the disruption of ADAR2 pathways. A total of nine potential lead compounds were shortlisted as plausible modulators of ADAR2.

Indexed as

Adenosine Deaminase InhibitorsCommunicable DiseasesNeoplasmsAdenosine DeaminaseBayes TheoremHumansMolecular Docking SimulationMolecular Dynamics SimulationRNA-Binding ProteinsADARB1 protein, humanAdenosine DeaminaseAdenosine Deaminase InhibitorsRNA-Binding Proteinsadenosine deaminases acting on RNA (ADAR)anti-ADAR2anxiety disordersautism spectrum disorder (ASD)cancerdepressionmolecular dockingmolecular dynamics simulationnatural products

Identifiers

PMID37047766
PMCPMC10095294
OpenAlexW4362671314

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.