DFT methods were utilized to investigate the relative energies of the ground state conformations of potential neuraminidase inhibitors. Global minima and local minima were obtained for all structures using the B3LYP/6-311++G** basis set. Each structure was bound to the N4 subtype of the neuraminidase protein using AutoDock 4.0 to find the lowest energy structure of the ligand-enzyme complex. Single point conformational energies of these bound ligands were then determined and compared to the minima of the unbound species to evaluate the efficacy of this method.

Conformational mapping of potential neuraminidase inhibitors

246th National Meeting (2013)

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