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Ligand trapping as a key mechanism governing drug residence time, binding affinity, and potency
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DOI：10.1016/j.drudis.2026.104694.png)
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Abstract
En 中文
• Predicting drug binding affinity and potency remains challenging from structural information alone. • Protein–ligand interactions involve multiple kinetic mechanisms, including lock-and-key, induced fit, conformational selection, and ligand trapping.Ligand trapping arises from conformational enclosure of the ligand within the binding site. • Formation of closed protein conformations can impose steric and energetic barriers that slow ligand dissociation and prolong residence time, thereby enhancing drug binding affinity and potency. • Targeting protein structural opening and closure may therefore provide new opportunities in drug discovery.
Keywords:
residence time
binding affinity
inhibitor potency
lock and key
induced fit
conformational selection
inhibitor trapping
magic methyl
drug design
Abl
imatinib
RAS
Src
PARP
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