Insulin is known to be one of the key peptide hormones responsible for homeostasis. Its main role is to maintain the constant level of glucose in the blood by inducing the uptake of this sugar into the cells. This kind of action is possible due to the existence of metabolic cascades, which start from the binding of the insulin molecule to the membrane receptors and result in the activation of the membrane glucose transporters. Disruptions in the operation of this system lead to the development of many diseases, diabetes being one of the most recent. In the treatment of the mentioned disease, human insulin or proteins with a structure very similar to the natural hormone and mimicking its hypoglycemic effect (insulin analogs) are used.
The aim of the project, which results are presented on the poster, was to study the interactions of innovative recombinant insulin analogs, designed to have a prolonged time of action, with cell surface receptors – insulin receptor isoforms A and B (IR-A, IR-B) and insulin growth factor I receptor (IGF1R). It allowed us to check how insulin analogs with sequences only slightly different from natural hormone differ in their characteristics of receptor binding and the resulting observed biological effect, understood as their ability to activate metabolic and /or (possibly) mitogenic cascades.
The poster presents results obtained during the study on analog-receptor interactions carried out for a relatively large group of compounds of comparable primary protein structure using MP-SPR surface plasma resonance technique.