The protein behind Type 2 diabetes has finally been caught in the act, and could lead to a breakthrough in treatment.
More than 400 million people live with diabetes around the world, and the majority have Type 2—which develops when the body cannot produce enough insulin or when the insulin produced does not work properly.
The architecture of amyloid fibrils, a fibre-like structure that is the hallmark for Type 2 diabetes, has now been observed for the first time by scientists, according to a 2020 study published in Nature Structural and Molecular Biology.
Amyloid fibrils are produced from “clumps” of the peptide protein Amylin, which regulates the body’s glucose levels.
Study author Professor Neil Ranson, of the University of Leeds, said the finding is “really exciting” because it “is crucial in understanding the disease process… with these structures we’re getting the first glimpse at what might be going on.
The latest electron microscope technology, known as cryo-electron microscopy, was used to visualise the structure of the fibres.
Protein samples were frozen and then analyzed to a resolution where individual atoms can be observed.
People with early-onset Type 2 diabetes have a specific genetic variant of amyloid fibrils known as S20G. The researchers compared S20G with amyloid fibrils found in the general population, which they call the wild-type.
How amylin molecules stackup to form fibrils was observed by analyzing thousands of images.
The molecules formed intricate structures like rungs in a ladder, the researchers found.
The wild type fibrils, however, had two copies of amylin per rung, whereas some of the S20G had three, suggesting fibrils can form templates onto which more copies of amylin can lock.
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It would also explain why the S20G-variant protein lumps together more quickly and why it is linked to the rapid onset of Type 2 diabetes.
A Breakthrough For More Amyloid Diseases
Co-author Professor Sheena Radford, of the Astbury Centre, added that the breakthrough is important, “Not just for understanding amylin—but for understanding many amyloid diseases in which run-away fibril formation occurs.”
The build up of amyloid fibrils is also linked to other diseases such such as Alzheimer’s, Parkinson’s and Huntington’s Disease.
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A better understanding of amyloid fibrils structure could, then, pave the way to better diagnosis treatments for the millions of people who will suffer from amyloid diseases. That’s exciting news indeed.
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