Abstract
Interactions of azodicarbonamide (ADA) species with zinc-containing sites, which mimic the zinc finger domains of the HIV-1 nucleocapsid protein (NCp7), have been investigated by quantum chemistry tools in order to provide theoretical insights into recent experimental findings. In the latter, reactions of ADA with NCp7 lead to destabilization of the zinc coordination sphere followed by HIV inhibition. In this work, energy profiles for the interactions of neutral and protonated ADA species with the Zn binding site have been calculated at the density functional theory level in the B3LYP approximation. The calculations show that the ADA molecule, protonated at the central nitrogen atom, reacts without activation barrier with the model zinc binding site, destructing the metal coordination sphere, while interactions of other ADA species do not lead to modification of the metal site.
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