ArticleMolecules (Basel, Switzerland)2024
Machine Learning Methods as a Cost-Effective Alternative to Physics-Based Binding Free Energy Calculations.
Article in Molecules (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- A Multi-Scale Computational Framework for Anti-Persister Tuberculosis Drug Discovery.Chemical biology & drug design · 2026Review
- Design, In Silico, and Experimental Evaluation of Novel Naproxen-Azetidinone Hybrids as Selective COX-2 Inhibitors.Molecules (Basel, Switzerland) · 2025Article
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Authors and funding
3 authors.
Funding
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Abstract
The rank ordering of ligands remains one of the most attractive challenges in drug discovery. While physics-based in silico binding affinity methods dominate the field, they still have problems, which largely revolve around forcefield accuracy and sampling. Recent advances in machine learning have gained traction for protein-ligand binding affinity predictions in early drug discovery programs. In this article, we perform retrospective binding free energy evaluations for 172 compounds from our internal collection spread over four different protein targets and five congeneric ligand series. We compared multiple state-of-the-art free energy methods ranging from physics-based methods with different levels of complexity and conformational sampling to state-of-the-art machine-learning-based methods that were available to us. Overall, we found that physics-based methods behaved particularly well when the ligand perturbations were made in the solvation region, and they did not perform as well when accounting for large conformational changes in protein active sites. On the other end, machine-learning-based methods offer a good cost-effective alternative for binding free energy calculations, but the accuracy of their predictions is highly dependent on the experimental data available for training the model.
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