Impact of the Halogen PB Radii in the Estimation of Protein-Ligand Binding Energies Using MM-PBSA Calculations

Andreia Fortuna; Paulo J. Costa

doi:10.1039/d5cp03537f

January 1, 2026Physical Chemistry Chemical Physics

Impact of the Halogen PB Radii in the Estimation of Protein-Ligand Binding Energies Using MM-PBSA Calculations

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Key Points

The research aims to analyze how halogen PB radii influence the estimation of protein-ligand binding energies using MM-PBSA calculations.
Utilized MM-PBSA (Molecular Mechanics Poisson-Boltzmann Surface Area) calculations.
Compared binding energies of halogenated versus non-halogenated ligands.
Investigated different halogen PB radii in protein-ligand interactions.
Halogen PB radii significantly impact the predicted binding energies.
Halogen bonding was shown to enhance binding affinity under specific conditions.
Adjustments in PB radii improved the accuracy of the binding energy estimations.

Implication

Halogenation affects protein-ligand binding energies in drug design, suggesting implications for ADME properties.

Abstract

Halogenation is a widely used strategy in drug design, not only to improve ADME properties but also because halogens can engage in halogen bonds (XBs) with biological targets. To predict...

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Cite This Study

Fortuna et al. (2026) studied this question.

synapsesocial.com/papers/69ba427c4e9516ffd37a2d69 https://doi.org/10.1039/d5cp03537f

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Impact of the Halogen PB Radii in the Estimation of Protein-Ligand Binding Energies Using MM-PBSA Calculations

Key Points

Implication

Abstract

Discussion

Cite This Study

Impact of the Halogen PB Radii in the Estimation of Protein-Ligand Binding Energies Using MM-PBSA Calculations

Key Points

Implication

Abstract

Discussion

Cite This Study

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