Chemists at the University of Wisconsin-Madison have developed a novel analytical tool that is able to measure molecular structures quickly and accurately that it can catch moving proteins in mid-fold and see the shapes of intermediate steps through a method known as two-dimensional infrared spectroscopy (2-D IR).

What makes the tool more exciting because its first applications of the technique will be used to "take a picture" of the contorted form of human protein implicated in type 2 diabetes.

The said human protein is the protein hIAPP (human islet amyloid polypeptide), found in toxic clumps and is normally produced by the very same cells that make insulin.

These toxic clumps of protein hIAPP have been previously linked to pancreatic damage in type II diabetes.

According to UW-Madison chemistry professor Martin Zanni:

"No matter how fast they're moving, we can take pictures of them. Without the automated method, such experiments would be nearly impossible.

In time, automated 2-D IR spectroscopy will become a common analytical technique, widely available in university and industrial research laboratories around the world."

Using the said tool, the researchers obtained a single structural scan of hIAPP in less than a second which is actually more than 500 times faster than was previously possible.

Also, the technique has potential applications in other human diseases like Alzheimer's disease and Huntington's disease.

Wouldn't that be the day?! When we can just pop a pill to prevent such proteins from getting contorted into forms that will lead to diabetes or we can all undergo a simple diagnostic test that says, "hey! Your hIAPP proteins are about to get distorted, putting you at risk for diabetes...so you better pop this pill now."

It will still be long shot, but at this point at least we are on the way to getting there.

Read the full report.

[In photo: Insulin prevented formation of fibrils visible by EM: Samples of insulin (50 mM) and hIAPP (75 mM) were incubated separately or together for 24 h (A) hIAPP readily formed fibrils. (B) A mixture of hIAPP and human insulin resulted in the formation of amorphous aggregates. No precipitate was seen with insulin alone. Scale bars, 200 nm. Credit: Biochemical Journal (2004) Volume 377, 709-716]