ArticleJournal of chemical information and modeling2025
Estimation of Absolute Binding Free Energies for Drugs That Bind Multiple Proteins.
Article in Journal of chemical information and modeling, 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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Who cites it
3 citing papers in PubMed.
- Absolute Binding Free Energy Calculations between the SARS-CoV-2 Main Protease and 130 Drug Leads Using Implicit Ligand Theory.Journal of chemical information and modeling · 2026Article
- BindFlow: A Free, User-Friendly Pipeline for Absolute Binding Free Energy Calculations Using Free Energy Perturbation or MM(PB/GB)SA.Journal of chemical theory and computation · 2026Article
- Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Gibbs energy of binding (absolute binding free energy, ABFE) of a drug to proteins in the body determines the drug's affinity to its molecular target and its selectivity. ABFE is challenging to measure, and experimental values are not available for many proteins together with potential drugs and other molecules that bind them. Accurate means of calculating such values are, therefore, highly in demand. Realizing that toxicity and side effects are closely related to off-target binding, here we calculate the ABFE of two drugs, each to multiple proteins, in order to examine whether it is possible to carry out such calculations and achieve the required accuracy. The methods that were used were free energy perturbation with replica exchange molecular dynamics (FEP/REMD) and density functional theory (DFT) with a cluster approach and a simplified model. DFT calculations were supplemented with energy decomposition analysis (EDA). The accuracy of each method is discussed, and suggestions are made for the approach toward better ABFE calculations.
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Registered trials
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