Enhancing binding affinity predictions through efficient sampling with a re-engineered BAR method: a test on GPCR targets

Computational approaches for predicting the binding affinity of ligand-receptor complex structures often fail to validate experimental results satisfactorily due to insufficient sampling. To address these challenges, recent emphasis has been placed on the re-sampling of new trajectories. In this study, we propose a simulation protocol that achieves efficient sampling by re-engineering the widely used Bennett acceptance ratio (BAR) method as a representative approach. We tested its efficacy across various membrane protein targets, including G-protein coupled receptors (GPCRs) with diverse structural landscapes and experimentally validated binding affinities, to verify its efficient applicability. Subsequently, using BAR-based binding free energy calculations, we confirmed correlations with experimental data, demonstrating the validity and performance of this computational approach.

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Publication Details

Journal
Chemical Science
Published
2025-01-01
DOI
https://doi.org/10.1039/d5sc01030f
Citations
2
Primary Topic
Receptor Mechanisms and Signaling
Type
article
Field-Weighted Citation Impact
1.61

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article

Enhancing binding affinity predictions through efficient sampling with a re-engineered BAR method: a test on GPCR targets

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2 citations
Chemical Science
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article

Enhancing binding affinity predictions through efficient sampling with a re-engineered BAR method: a test on GPCR targets

Art E. Cho, Jian Jeong, Sangbae Lee, Donghwan Kim, Minkyu Kim
article en
2 citations

Abstract

Computational approaches for predicting the binding affinity of ligand-receptor complex structures often fail to validate experimental results satisfactorily due to insufficient sampling. To address these challenges, recent emphasis has been placed on the re-sampling of new trajectories. In this study, we propose a simulation protocol that achieves efficient sampling by re-engineering the widely used Bennett acceptance ratio (BAR) method as a representative approach. We tested its efficacy across various membrane protein targets, including G-protein coupled receptors (GPCRs) with diverse structural landscapes and experimentally validated binding affinities, to verify its efficient applicability. Subsequently, using BAR-based binding free energy calculations, we confirmed correlations with experimental data, demonstrating the validity and performance of this computational approach.

Chemical ScienceVol. 16(25)
Korea University (KR)
National Research Foundation, National Research Foundation of Korea
Openalex Percentile: Top 17%
Receptor Mechanisms and Signaling
1.61
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