Researchers advance understanding of fibril inhibitors for diabetes therapy
In a paper published in March 2012 in the journal Nature Chemistry, Chemistry Professor Martin Zanni and Howard Curler Distinguished Professor and Hilldale Professor of Chemical and Biological Engineering Juan de Pablo examined amylin aggregation. Amylin is a polypeptide that can form amyloid fibrils, or deposits, in the pancreatic islet cells of Type II diabetes patients. There is considerable interest in identifying inhibitors to fibril formation because they eventually could lead to therapeutic strategies against Type II diabetes. However, a lack of structural information about amyloid–inhibitor complexes has prevented researchers from designing effective amyloid inhibitors. Using a combination of two-dimensional infrared spectroscopy and molecular simulations, Zanni, dePablo and their students showed that even seemingly intuitive inhibitors—in this case, rat amylin—actually may function through previously unknown, complex structural processes.