Molecular dynamics (MD) simulations for the prediction of chiral discrimination of N-acetylphenylalanine enantiomers by cyclomaltoheptaose (β-cyclodextrin, β-CD) based on the MM–PBSA (molecular mechanics–Poisson–Boltzmann surface area) approach Original R

Molecular dynamics (MD) simulations were performed for the prediction of chiral discrimination of N-acetylphenylalanine enantiomers by cyclomaltoheptaose (β-cyclodextrin, β-CD). Binding free energies and various conformational properties were obtained using by the MM–PBSA (molecular mechanics Poisson–Boltzmann/surface area) approach. The calculated relative difference (ΔΔGbinding) of binding free energy was in fine agreement with the experimentally determined value. The difference of rotameric distributions of guest N-acetylphenylalanine enantiomers complexed with the host, β-CD, was observed after the conformational analyses, suggesting that the conformational changes of guest captured within host cavity would be a decisive factor for enantiodifferentiation at a molecular level.