Abstract by Mikayla Twiggs

Personal Infomation

Presenter's Name

Mikayla Twiggs

Degree Level


Abstract Infomation


Chemistry and Biochemistry

Faculty Advisor

Roger Harrison


Dicopper Complexes as Influenza M2 Inhibitors


The influenza virus is most commonly combated by drugs that target sites vital to viral reproduction. The virus has become resistant to the previously-used adamantane based drugs and is becoming resistant to the neuraminidase-blocking drugs currently used. The M2 proton channel in the viral membrane is vital to replication and has been retained throughout viral mutation, making it a prime target for drugs. The M2 pore-lining M2 residue histidine 37 has been conserved without change, as it acts as the pH sensor that controls proton flow in and out of the virus. Previous research done by our lab showed that copper cation complexes bind strongly to this residue, preventing the virus from replicating. Synthesis of a new copper(II) organic complex as a possible influenza M2 channel blocker will be described. This novel copper compound will be synthesized through the substitution of glycine ethyl ester onto the aldehyde substituent of 2,6-dimethylformyl-4-methylphenol. This is followed by hydrolysis of the esters on the glycine arms and the addition of two copper cations to the final product. This final product will be the novel dicopper complex.