Search Here

Monitoring formation of amylin plaques with the help of 2-D IR spectroscopy, researchers have observed the creation of a temporary intermediate structures, according to a new study. The findings may explain why proteins aggregate into toxic plaques. 

"Figuring out how and why amyloid plaques form is exceedingly difficult, because one needs to follow the atomic shapes of the protein molecules as they assemble. Most tools in biology give either shapes or motions, but not both. We have been developing a new spectroscopic tool, called two-dimensional infrared spectroscopy, which can monitor the plaques as they form in a test tube," lead investigator Martin T. Zanni, PhD, of the Department of Chemistry at the University of Wisconsin-Madison said in the press release. 

Researchers applied the new technology to gain better understanding of the amyloid protein associated with type 2 diabetes. They followed many 2D IR spectra from one particular region over several hours. Eventually researchers were able to visualize the amylin as it progressed from monomers to fibers.

"We learned that, prior to making the plaques, the proteins first assemble into an unexpected and intriguing intermediate and organized structure," commented Dr. Zanni. 

 "I am not encouraging us to begin engineering our DNA to match that of rats, but our findings may help to develop plaque inhibitors or hormone replacement therapies for people suffering from type 2 diabetes, because we know the structure we want to avoid."

The study has been published in the current issue of Biomedical Spectroscopy and Imaging.