Synthesis and characterization of AibB8LysB28ProB29-insulin to study T a R conformations of insulin

According to the International Diabetes Federation, there were 285 million people in the age from 20 to 79 years suffering from diabetes on the planet in 2010. This means diabetes has become a global epidemic so the importace of insulin research is still growing. Insulin is a protein hormone that plays a key role in regulating blood glucose level which has a widespread impact on the whole metabolism. Insulin acts through binding of its monomeric form to the insulin receptor. At present, however, the active monomeric structure of insulin is still unknown. It is clear that insulin monomer must undergo structural changes upon binding to the insulin receptor as the residues crucial for the interaction are burried within the native form. According to studies of highly active hormon analogs there is an ample evidence that the C-terminal part of the B-chain is a dynamic element in insulin activation and receptor binding. Probably, there is also great importance of the B-chain N- terminus and the transition between T and R conformation. However, the exact significance of the T and R states of insulin remains unclear. In this work, a new insulin analog AibB8LysB28ProB29-insulin was prepared for the purpose of studying significance of the T and R conformations of insulin and their relationship to the active..