A new method for predicting binding affinity in computer-aided drug design.

J Aqvist; C Medina; J E Samuelsson

doi:10.1093/protein/7.3.385

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A new method for predicting binding affinity in computer-aided drug design.

J Aqvist·C Medina·J E Samuelsson

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Abstract

A new semi-empirical method for calculating free energies of binding from molecular dynamics (MD) simulations is presented. It is based on standard thermodynamic cycles and on a linear approximation of polar and non-polar free energy contributions from the corresponding MD averages. The method is tested on a set of endothiapepsin inhibitors and found to give accurate results both for absolute as well as relative free energies.

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Aspartic Acid Endopeptidases Binding Sites Computer Simulation Drug Design Electrochemistry Molecular Structure Protein Binding Thermodynamics Journal Article Research Support, Non-U.S. Gov't

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J Aqvist, C Medina, J E Samuelsson. 1994. A new method for predicting binding affinity in computer-aided drug design.. https://doi.org/10.1093/protein%2F7.3.385

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