Abstract by Ethan Damron
Chemistry and Biochemistry
Copper Amantadine-iminodiethylamine as an Influenza Inhibitor
Nearly 99.97% of influenza virus strains have a protein channel containing histidines that are known to tightly bind divalent cations. When a divalent cation binds to the imidazole group of histidines it could disrupt the M2 proton channel and cause the virus to become inactive. Further adjustments to the binding strength, and therefore amount of M2 channel block, of the cation can be made based on what ligand is attached to the metal. The use of divalent metal ions in influenza drugs could create a drug that is unlikely to become obsolete due to influenza mutations since almost all influenza strains have imidazole groups.