Unravelling the mysteries around type 2 diabetes

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For more than 30 years, scientists have been trying to unravel how a key molecule in itself binds to a chemical compound called amyloid, which is thought to play a role in the development of type 2 diabetes. affecting 300 million people worldwide.

A team of scientists at the University of Leeds, for the first time, were able to detect the gradual changes that take place in the islet amyloid polypeptide, or hIAPP, as it converts to amyloid.

They also discovered new compounds that can speed up or slow down performance.

In healthy people, HIAPP is secreted by the islets in the pancreas along with the hormone insulin and helps regulate blood glucose levels and the amount of food in the stomach. When hIAPP is inactive, it causes the formation of a protein-like substance called amyloid fibrils that kill the insulin-producing islands in the pancreas.

Amyloid fibrils are seen in people with type 2 diabetes although the exact mechanism by which they cause disease is not known.

The results of the study — Tuning the rate of aggregation of hIAPP into amyloid using small-molecule modulators of assembly — were published today in the journal. Environmental communication.

The paper not only describes the complex genetic mutations observed in the hIAPP organic matter while they are transformed into amyloid fibrils, but evolutionists also report that they have discovered two other compounds, expressed as molecular regulators, that can control the process: one compound slows it down, the other accelerates it .

These adaptive devices can be used as “chemical tools” to help scientists explore the path amyloid fibrils size and how and why they become toxic.

Essentially they provide a “starting point” to develop drugs that can inhibit or control amyloid fibril availability and assistance in rapid research to find treatment options for type 2 diabetes.

Sheena Radford, Associate Professor of Biology and Professor at the Astbury Institute of Biology in Leeds, who led the study, said: “This is an exciting and significant step forward in our efforts to understand and address amyloid disease and treatment of the disease: a major health issue that is growing rapidly.

“The drugs we have identified are the first and most important step for the development of micro-organisms in a disease that has been ignored by generational scientists.”

The research team looked at the common hIAPP in the community and the type of mutations found in people with mutations known as S20G that put them at risk of developing the type type 2 diabetes.

Formation of Amyloid fibril associated with disease

Understand amyloid fibril formation it is an important area of ​​medical research. The formation of fibrils is believed to be a factor in a range of life-threatening diseases including Alzheimer’s disease and Parkinson’s disease, as well as type 2 diabetes.

Professor Radford added: “The results are also very impressive as they open the door to use different methods of understanding others. amyloid diseases, most of which currently have no cure. ”


Evaluation of protein-associated protein structures


Learn more:
Adjust the amount of hIAPP binding to the amyloid using a small number of mass ions, Environmental communication (2022). DOI: 10.1038 / s41467-022-28660-7

Its formation
University of Leeds

hint: Reveal the secrets surrounding type 2 diabetes (2022, February 24) Retrieved 24 February 2022 from https://medicalxpress.com/news/2022-02-unravelling-mysteries-diabetes.html

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