Martin Zanni

My group develops and applies new methods of 2D infrared (2D IR) spectroscopy to study protein structures as they evolve. 2D IR is similar to 2D NMR, but rather than studying nuclear spins, we study vibrational modes (such as the amide-I vibration of a single amino acid in a protein backbone). In 2013, we used 2D IR to uncover an on-pathway toxic oligomeric intermediate of human islet amyloid polypeptide (hIAPP). Since then, we have characterized the structure and cytotoxicity of this intermediate and are using our in vitro results to create a new mouse model for type II diabetes, in collaboration with Alan Attie and the gene- editing facility in the UW-Madison Biotechnology Center. We are now examining the impact of oligomers and fibrils on islet and acinar cell function. Recently, we have developed 2D IR bioimaging, a form of microscopy that uses a moving stage to scan sections of human and mouse tissues, creating a location-resolved map of protein structure within these tissues.