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

摘要

Molecular dynamics (MD) simulations were performed for the prediction of chiral discrimination of N-acetylphenyl-alanine enantiomers by cyclomaltoheptaose (beta-cyclodextrin,beta-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 (DELTA DELTAG_(binding) 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,beta-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.