Evidence map›Paper›PMID 37940790›Full record

ArticleThe protein journal2024

Repurposing of Strychnine as the Potential Inhibitors of Aldo-keto Reductase Family 1 Members B1 and B10: Computational Modeling and Pharmacokinetic Analysis.

Muhammad Sarfraz, Mubashir Aziz, Saira Afzal, Pervaiz Ali Channar, Bshra A Alsfouk, Ghulam Abbas Kandhro, Sidra Hassan, Ahlam Sultan, Asad Hamad, Mosab Arafat and 4 more

Abstract read
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Article in The protein journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. 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

14 authors at 8 institutions in 4 countries.

Muhammad SarfrazCollege of Pharmacy, Al Ain University, Al Ain Campus, 64141, Al Ain, United Arab Emirates.
Mubashir AzizDepartment of Pharmaceutical Chemistry, Faculty of Pharmacy, The Islamia University of Bahawalpur, Bahawalpur, 63100, Pakistan.
Saira AfzalFaculty of Pharmacy, The University of Lahore, Lahore, Pakistan.
Pervaiz Ali ChannarDepartment of Basic Sciences, Mathematics and Humanities, Dawood University of Engineering and Technology, Karachi, 74800, Pakistan.
Bshra A AlsfoukDepartment of Pharmaceutical Sciences, College of Pharmacy, Princess Nourah bint Abdulrahman University, P.O Box 84428, 11671, Riyadh, Saudi Arabia.
Ghulam Abbas KandhroDepartment of Basic Sciences, Mathematics and Humanities, Dawood University of Engineering and Technology, Karachi, 74800, Pakistan.
Sidra HassanBahawalpur College of Pharmacy, Bahawalpur Medical and Dental College, Bahawalpur, Pakistan.
Ahlam SultanDepartment of Pharmaceutical Sciences, College of Pharmacy, Princess Nourah bint Abdulrahman University, P.O Box 84428, 11671, Riyadh, Saudi Arabia.
Asad HamadFaculty of Pharmacy, Grand Asian University, Sialkot, 51310, Punjab, Pakistan.
Mosab ArafatCollege of Pharmacy, Al Ain University, Al Ain Campus, 64141, Al Ain, United Arab Emirates.
Muhammad Naeem QaiserCollege of Pharmacy, University of Sargodha, Sargodha, Punjab, Pakistan.
Aftab AhmedDepartment of Pharmaceutical Chemistry, Faculty of Pharmacy, The Islamia University of Bahawalpur, Bahawalpur, 63100, Pakistan.
Farhan SiddiqueDepartment of Chemistry and Biochemistry, Texas Tech Universit, Lubboc, TX, 79409-1061, USA.
Syeda Abida EjazDepartment of Pharmaceutical Chemistry, Faculty of Pharmacy, The Islamia University of Bahawalpur, Bahawalpur, 63100, Pakistan. abida.ejaz@iub.edu.pk.
Islamia University of Bahawalpur · PKAl Ain University · AEDawood University of Engineering and Technology · PKPrincess Nourah bint Abdulrahman University · SABahawal Victoria Hospital · PKTexas Tech University · USUniversity of Lahore · PKUniversity of Sargodha · PK

Funding

Princess Nourah Bint Abdulrahman University PNURSP2023R142
6 · The paper itself

Abstract

AKR1B1 and AKR1B10 are important members of aldo-keto reductase family which plays a significant role in cancer progression by modulating cellular metabolism. These enzymes are involved in various metabolic processes, including the synthesis and metabolism of hormones, detoxification of reactive aldehydes, and the reduction of various endogenous and exogenous compounds. This study aimed to explore the potential of strychnine as an anticancer agent by targeting AKR1B1 and AKR1B10 via drug repurposing approach. To assess the drug-like properties of strychnine, a physiologically based pharmacokinetic (PKPB) model and High Throughput Pharmacokinetics (HTPK) approach were employed. The obtained results fell within the expected range for drug molecules, confirming its suitability for further investigation. Additionally, density functional theory (DFT) studies were conducted to gain insight into the electronic properties contributing to the drug molecule's reactivity. Building upon the promising DFT results, molecular docking analysis using the AutoDock tool was performed to examine the binding interactions between strychnine and the proposed targets, AKR1B1 and AKR1B10. Findings from the molecular docking studies suggested a higher probability of strychnine acting as an inhibitor of AKR1B1 and AKR1B10 with docking scores of - 30.84 and - 29.36 kJ/mol respectively. To validate the stability of the protein-ligand complex, Molecular Dynamic Simulation (MDS) studies were conducted, revealing the formation of a stable complex between the enzymes and strychnine. This comprehensive approach sheds light on the potential effectiveness of strychnine as a treatment for breast, lung, liver, and pancreatic cancers, as well as related malignancies. The novel insights gained from the physiologically based pharmacokinetic modeling, density functional theory, molecular docking, and molecular dynamics simulations collectively support the prospect of strychnine as a promising molecule for anticancer therapy. Further investigations are warranted to validate these findings and explore the therapeutic potential of strychnine in preclinical and clinical settings.

Indexed as

Aldehyde ReductaseAldo-Keto ReductasesDrug RepositioningMolecular Docking SimulationStrychnineAntineoplastic AgentsEnzyme InhibitorsHumansMolecular Dynamics SimulationAKR1B10 protein, humanAKR1B1 protein, humanAldehyde ReductaseAldo-Keto ReductasesAntineoplastic AgentsEnzyme InhibitorsStrychnineADMETCancersGastroPlusMD simulationsMolecular dockingStrychnine

Identifiers

PMID37940790
OpenAlexW4388488160

What OpenQuestion holds

Textmetadata
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.