ArticleNature communications2025
Molecular basis of the functional conflict between chloroquine and peptide transport in the Malaria parasite chloroquine resistance transporter PfCRT.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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.
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Who cites it
3 citing papers in PubMed.
- A Multidimensional Analysis of the Bimodal Piperaquine Response inbioRxiv : the preprint server for biology · 2026Article
- Gain-of-function PfAAT1 mutations compensate for impaired PfCRT function inResearch square · 2026Article
- Collateral hypersensitivity between ZY19489 and piperaquine neutralizes PfCRT-mediated drug efflux and Plasmodium falciparum resistance.Nature communications · 2026Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Plasmodium falciparum chloroquine resistance transporter (PfCRT) is a key protein contributing to resistance against the antimalarial chloroquine (CQ). Mutations such as K76T enable PfCRT to transport CQ away from its target in the parasite's digestive vacuole, but this comes at a cost to its natural peptide transport function. This creates fitness costs which can drive changes to drug susceptibility in parasite populations, but the molecular basis of this is not well understood. To investigate, here we run 130 μs of molecular dynamics simulations of CQ-sensitive and CQ-resistant PfCRT isoforms with CQ and peptide substrates. We identify the CQ binding site and characterized diverse peptide binding modes. The K76T mutation allows CQ to access the binding site but disrupts peptide binding, highlighting the importance of cavity charge in determining substrate specificity. This study provides insight into PfCRT polyspecific peptide transport and will aid in rational, structure-based inhibitor design.
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