Evidence map›Paper›PMID 41951873›Full record

ArticleEuropean journal of drug metabolism and pharmacokinetics2026

The Effect of Arylquinoline-Based EGFR and FAK Kinase Inhibitors on the Activity of Major Cytochrome P450 Enzymes.

Fawzy Elbarbry, Michael Espiritu, Bethany Hecker, Mostafa M Elbadawi, Wagdy M Eldehna

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Article in European journal of drug metabolism and pharmacokinetics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Fawzy ElbarbrySchool of Pharmacy, Pacific University Oregon, 222 SE 8thAve., Hillsboro, OR, 97123, USA. Fawzy.elbarbry@pacificu.edu.ORCID http://orcid.org/0000-0002-5238-2712
Michael EspirituSchool of Pharmacy, Pacific University Oregon, 222 SE 8thAve., Hillsboro, OR, 97123, USA.
Bethany HeckerSchool of Pharmacy, Pacific University Oregon, 222 SE 8thAve., Hillsboro, OR, 97123, USA.
Mostafa M ElbadawiDepartment of Pharmaceutical Chemistry, Faculty of Pharmacy, Kafrelsheikh University, P.O. Box 33516, Kafrelsheikh City, Egypt.
Wagdy M EldehnaDepartment of Pharmaceutical Chemistry, Faculty of Pharmacy, Kafrelsheikh University, P.O. Box 33516, Kafrelsheikh City, Egypt.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

BACKGROUND AND

objectiveThe cytochrome P450 (CYP) system plays a central role in drug metabolism and pharmacokinetic variability, influencing drug-drug interaction risk. The newly synthesized 4-propoxy-2-arylquinoline derivatives (MW1-3) are dual inhibitors of epidermal growth factor receptor (EGFR) and focal adhesion kinase (FAK) with potent anticancer activity. This study aimed to assess their potential inhibitory effects on major human CYP enzymes to predict metabolic liabilities and interaction risks.

methodsInhibitory effects of MW1-3 were evaluated against CYP1A2, CYP2A6, CYP2C9, CYP2C19, CYP2D6, CYP2E1, and CYP3A4 using pooled human liver microsomes and probe substrates quantified by validated liquid chromatography with tandem mass spectrometry (LC-MS/MS) and high-performance liquid chromatography-ultraviolet (HPLC-UV) assays. Molecular docking was performed with the seven CYP enzymes to estimate binding affinities and identify possible enzyme-ligand interactions.

resultsAll the compounds showed negligible inhibition of CYP1A2 with half-maximal inhibitory concentrations (IC

conclusionMW1-3 exhibit selective and differential inhibition profiles toward major CYP enzymes, with CYP2A6, CYP2D6, and CYP2E1 being most affected. These findings provide essential preclinical insights for predicting potential drug-drug interactions and guiding the safe development of these arylquinoline-based anticancer agents.

Indexed as

Cytochrome P-450 Enzyme InhibitorsCytochrome P-450 Enzyme SystemErbB ReceptorsProtein Kinase InhibitorsQuinolinesDrug InteractionsHumansMicrosomes, LiverMolecular Docking SimulationTyrosine Kinase InhibitorsCytochrome P-450 Enzyme InhibitorsCytochrome P-450 Enzyme SystemEGFR protein, humanErbB ReceptorsProtein Kinase InhibitorsQuinolinesTyrosine Kinase Inhibitors

Identifiers

PMID41951873

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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.