Research data for article: Gold electrode modified with proteoliposome-derived bilayer for electrochemical studies of HMG‑CoA reductase and its inhibition

Electrochemical methods (cyclic voltammetry and electrochemical impedance spectroscopy) were used to monitor changes in the catalytic properties or activity of membrane protein, HMG-CoA reductase (HMGR) in the presence of activators or inhibitors. The protein and its related coenzyme (HMG-CoA) were incorporated into a lipid bilayer obtained by spreading proteoliposomes on the surface of a gold electrode modified with thioglucose. The reconstitution of HMG-CoA reductase was investigated by following the NADP + reduction on the electrode using cyclic voltammetry (CV) and electrochemical impedance spectroscopy (EIS). The activity of HMGR was studied over time and in the presence of an inhibitor (fluvastatin). The inhibitory effect was electrochemically evaluated by monitoring the decrease of NADP + reduction current and changes in the impedance parameters of the HMGR-proteoliposome-derived bilayer.