Evidence map›Paper›PMID 38893537›Full record

ArticleMolecules (Basel, Switzerland)2024

The Discovery of Selective Protein Arginine Methyltransferase 5 Inhibitors in the Management of β-Thalassemia through Computational Methods.

Bishant Pokharel, Yuvaraj Ravikumar, Lavanyasri Rathinavel, Teera Chewonarin, Monsicha Pongpom, Wachiraporn Tipsuwan, Pimpisid Koonyosying, Somdet Srichairatanakool

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
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

8 authors.

Bishant PokharelDepartment of Biochemistry, Faculty of Medicine, Chiang Mai University, Chiang Mai 50200, Thailand.ORCID 0009-0008-6638-113X
Yuvaraj RavikumarDepartment of Biochemistry, Faculty of Medicine, Chiang Mai University, Chiang Mai 50200, Thailand.
Lavanyasri RathinavelDepartment of Biotechnology, Mercy College, Palakkad 678006, India.ORCID 0000-0002-7307-8058
Teera ChewonarinDepartment of Biochemistry, Faculty of Medicine, Chiang Mai University, Chiang Mai 50200, Thailand.ORCID 0000-0001-9044-3777
Monsicha PongpomDepartment of Microbiology, Faculty of Medicine, Chiang Mai University, Chiang Mai 50200, Thailand.ORCID 0000-0003-4822-5850
Wachiraporn TipsuwanDivision of Biochemistry, School of Medical Science, University of Phayao, Phayao 5600, Thailand.
Pimpisid KoonyosyingDepartment of Biochemistry, Faculty of Medicine, Chiang Mai University, Chiang Mai 50200, Thailand.
Somdet SrichairatanakoolDepartment of Biochemistry, Faculty of Medicine, Chiang Mai University, Chiang Mai 50200, Thailand.ORCID 0000-0002-5706-8781

Funding

Chiang Mai University, Thailand TGCMU2566P010/2566CMU Faculty of Medicine Fund, Chiang Mai University, Thailand BIO-2566-0574Post-Doctoral Fellowship 2022 (Reinventing University) through Dr. Yuvaraj Ravikumar, Chiang Mai University, Thailand PD2565Presidential Ph.D. Scholarship, Chiang Mai University, Thailand 2563-009
6 · The paper itself

Abstract

β-Thalassemia is an inherited genetic disorder associated with β-globin chain synthesis, which ultimately becomes anemia. Adenosine-2,3-dialdehyde, by inhibiting arginine methyl transferase 5 (PRMT5), can induce fetal hemoglobin (HbF) levels. Hence, the materialization of PRMT5 inhibitors is considered a promising therapy in the management of β-thalassemia. This study conducted a virtual screening of certain compounds similar to 5'-deoxy-5'methyladenosine (3XV) using the PubChem database. The top 10 compounds were chosen based on the best docking scores, while their interactions with the PRMT5 active site were analyzed. Further, the top two compounds demonstrating the lowest binding energy were subjected to drug-likeness analysis and pharmacokinetic property predictions, followed by molecular dynamics simulation studies. Based on the molecular mechanics Poisson-Boltzmann surface area (MM-PBSA) score and molecular interactions, (3R,4S)-2-(6-aminopurin-9-yl)-5-[(4-ethylcyclohexyl)sulfanylmethyl]oxolane-3,4-diol (TOP1) and 2-(6-Aminopurin-9-yl)-5-[(6-aminopurin-9-yl)methylsulfanylmethyl]oxolane-3,4-diol (TOP2) were identified as potential hit compounds, while TOP1 exhibited higher binding affinity and stabler binding capabilities than TOP2 during molecular dynamics simulation (MDS) analysis. Taken together, the outcomes of our study could aid researchers in identifying promising PRMT5 inhibitors. Moreover, further investigations through in vivo and in vitro experiments would unquestionably confirm that this compound could be employed as a therapeutic drug in the management of β-thalassemia.

Indexed as

beta-ThalassemiaEnzyme InhibitorsMolecular Docking SimulationMolecular Dynamics SimulationProtein-Arginine N-MethyltransferasesAdenosineCatalytic DomainDrug DiscoveryHumansProtein BindingAdenosineEnzyme InhibitorsPRMT5 protein, humanProtein-Arginine N-Methyltransferasesdynamicsfetal hemoglobinmolecular dockingPRMT5 inhibitorssimulationsβ-thalassemia

Identifiers

PMID38893537
PMCPMC11173459

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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.