In silico modeling of the interactions of the plasmodium falciparum resistance proteins PfCRT and PfMDR1 to selected antimalarial drugs

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ID: 284704
2025
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Abstract
The persistent threat of malaria, caused by the Plasmodium falciparum parasite, is significantly exacerbated by the rapid emergence and spread of drug resistance, particularly against artemisinin-based combination therapies (ACTs). This study utilized in silico modeling to investigate the molecular mechanisms underlying drug resistance, focusing on the impact of specific mutations in two crucial malaria-associated protein: Plasmodium falciparum Chloroquine Resistance Transporter (PfCRT) and Plasmodium falciparum Multidrug Resistance 1 (PfMDR1). PfCRT is a transmembrane protein in the parasite’s digestive vacuole that functions primarily as an efflux pump, removing certain drugs from the parasite's digestive vacuole, which can lead to drug resistance; while PfMDR1 is also a transmembrane protein which acts as an influx pump and its mutations can reduce transported drugs into the digestive vacuole. By employing docking simulations, the study aimed to predict the binding affinities of six clinically relevant antimalarial drugs—artemisinin, artesunate, doxycycline, mefloquine, artemether, and lumefantrine—to both wild-type and mutant protein structures. The findings revealed notable variations in drug-protein interactions, providing insights into potential resistance mechanisms. The findings revealed that mutations in PfCRT (K76T and C101F) altered the predicted binding affinity of artemisinin derivatives, potentially contributing to artemisinin resistance. Notably, the consistently low predicted binding affinities observed for chloroquine across both wild-type and mutant PfCRT proteins may add insights into the established role of this gene in chloroquine resistance. For PfMDR1, the N86Y and Y184F mutations reduced the predicted binding of drug components in ACTs (lumefantrine, mefloquine, doxycycline, artesunate), suggesting possible roles in the mechanisms for resistance to these drugs. Additionally, the study found that these mutations may affect protein stability. This could further affect drug interactions and possibly contribute to antimalarial drug resistance
Reference Key
persistent_1760653442_68f1708201915 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Tuazon, Lyam Arley Bernardo
Journal Malay Journal
Year 2025
DOI
DOI not found
URL
https://animorepository.dlsu.edu.ph/etdb_bio/102
Keywords Keywords not found

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