Assessment reveals P-glycoprotein inhibition and substrate transport in the blood-brain barrier, suggesting new insights into drug resistance.
We explored the pharmacology of the P-glycoprotein (P-gp) efflux pump and its role in multidrug resistance. We used Protein Data Bank (PDB) database mining and the artificial intelligence (AI) model Boltz-2.1.1, developed for simultaneous structure and affinity prediction, to explore the multimeric nature of recent P-gp inhibitors. We construct a MARTINI coarse-grained (CG) force field description of P-gp embedded in a model of the endothelial blood–brain barrier. We found that recent P-gp inhibitors have been captured in either monomeric, dimeric, or trimeric states. Our CG model demonstrates the ability of P-gp substrates to permeate and transition across the BBB bilayer. We report a multimodal binding model of P-gp inhibition in which later generations of inhibitors are found in dimeric and trimeric states. We report analyses of P-gp substrates that point to an extended binding surface that explains how P-gp can bind over 300 substrates non-selectively. Our coarse-grained model of substrate permeation into membranes expressing P-gp shows benchmarking similarities to prior atomistic models and provide new insights on far longer timescales.
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Jorgensen et al. (2025) studied this question.
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