期刊
BIOORGANIC & MEDICINAL CHEMISTRY
卷 14, 期 8, 页码 2636-2641出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2005.11.047
关键词
binding free energies; molecular dynamics simulations; surface accessible solvent area; adenosine deaminase inhibitors
The interactions between four inhibitors and adenosine deaminase (ADA) were examined by calculating their binding free energies after molecular dynamics simulations. A bonded model was used to represent the electrostatic potentials of the zinc coordination site. The charge distribution of the model was derived by using a two-stage electrostatic potential fitting calculations. The calculated binding free energies are in good agreement with the experimental data and the ranking of binding affinities is well reproduced. Notably, our findings suggest that non-polar contributions play ail important role for ADA-inhibitor interactions. (c) 2006 Elsevier Ltd. All rights reserved.
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