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Electrostatic interactions between small molecules and their respective receptors are essential for molecular recognition and are also key contributors to the binding free energy. Assessing the electrostatic match of protein-ligand complexes therefore provides important insights into why ligands bind and what can be changed to improve binding. Ideally, ligand and protein electrostatic potentials at the protein-ligand interaction interface should maximize their complementarity while minimizing desolvation penalties. In this work, we present a fast and efficient tool to calculate and visualize the electrostatic complementarity (EC) of protein-ligand complexes. Using several benchmark sets compiled from mainly electrostatically driven SAR, including data of the PPI target XIAP and the GPCR mGLU5, we demonstrate that the EC method can visualize, rationalize, and predict electrostatically driven ligand affinity changes and help to predict compound selectivity. The methodology presented here for analysis of electrostatic complementarity is a powerful and versatile tool for drug design.

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 Cresset provide a variety of software packages to support small molecule design, built on the foundation of their extended forcefield XED forcefield. When I first reviewed a couple of Cresset products FieldView, FieldAlign and Forge the forcefield was...