Binding of colicins A and E1 to purified ToIA domains

A research on the binding of colicins A and E1 and their interaction with ToIA soluble derivatives was conducted. Research methodologies included plasmid constructs, purification of ToIA derivatives and N-terminal domains of colicins A and E1, Western blotting and peptide analysis. Results showed that the N-terminal domain of colicin E1 and A can interact with the C terminal of TolA. Furthermore, the binding of colicins A and E1 to ToIA were estimated by surface plasmon resonance and were shown to be similar.