title: Binding free energy calculations of adenosine deaminase inhibitors.
abstract: 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 an important role for ADA-inhibitor interactions.
authors.affiliation: Dipartimento di Scienze Farmaceutiche, Università di Pisa, 56126 Pisa, Italy.
authors.forename: Alessio
authors.initials: A
authors.lastname: Coi
authors.forename: Marco
authors.initials: M
authors.lastname: Tonelli
authors.forename: Maria Luisa
authors.initials: ML
authors.lastname: Ganadu
authors.forename: Anna Maria
authors.initials: AM
authors.lastname: Bianucci
mesh_terms: D058892:Adenosine Deaminase Inhibitors; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D008958:Models, Molecular; D055672:Static Electricity
chemical_list: D058892:Adenosine Deaminase Inhibitors; D004791:Enzyme Inhibitors