Metallothionein is intracellular metal binding protein. It can bind essential zinc ions and also toxic metals like cadmium.
In cancer research the problem of resistance of cancer cells against anticancer drugs was described. In this study we optimized an electrochemical method for exploring the differences in electrochemical signals in dependence on amino acid sequence in metallothionein.
For this purpose we selected the number of fragments based on bioinformatic processing, synthesized them and made high throughput electrochemical analysis. Designed electrochemical analysis was based on automated flow injection analysis with amperometric detector using Coulochem III.
Detection was carried out by glassy carbon electrode. We measured hydrodynamic voltammograms (HDVs) for 23 selected metallothionein fragments within the potential range from 100 to 1200 mV.
We estimated the maxima of oxidation by processing of cumulative HDV. The oxidation maxima were dependent on amino acid composition, whereas fragments from human isoforms and some saltwater fishes' species had the highest maxima (900 mV).
On the opposite side fragments of other mammals like horse, mouse and bull had the lowest potential maxima (700 mV). This should be related with the binding capacity for metal ions.