Thermalin rapid-acting insulins hinge on B-Chain position B24
Cleveland, OH and Boston, MA – January 23, 2013 – An article has been published in the journal Nature that provides a rationale for the unique and advantageous activity of several of the insulin analogs under development at Thermalin.
The article, co-authored by Thermalin founder and Chief Science Officer Michael Weiss in an international collaboration, reported a breakthrough in the understanding of how insulin interacts with the insulin receptor on cell surface membranes.
Long an important scientific mystery, scientists have tried for dozens of years to figure out how insulin and related growth factors fit into the insulin receptor “keyhole” to enable uptake of glucose into cells and prevent the hyperglycemia associated with diabetes. For the first time, 90 years after the discovery of insulin, researchers have captured the structural image of the interaction of insulin with its primary binding site on the insulin receptor. The article reveals important details of the interaction and their implications for how the insulin signal is transmitted.
According to Dr. Weiss, “the research has provided insight into the molecular functioning of the insulin receptor and its homolog, the type 1 insulin-like growth factor receptor, which is implicated in tumor growth. This understanding has direct relevance to the structural bases of improved insulin analogues.”
Full Press Release here:
very interesting work.
What I am interested to know is: Can the cell sensor site throttle response to the available insulin to control glucose transfer from blood stream based upon how full the target cell is full of glucose already.
Based upon how full of glucose the target cell is?
I'd imagine no, since the movement of glucose into or out of a cell is driven by diffusion and, therefore, glucose concentration difference between the cell and the external medium anyway. I'd imagine that the net movement of glucose is going to depend on the rate of glucose use by the cell, how fast hexokinase can work, how much glucose is in the external environment, and keeping the transport proteins open with insulin.