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Amyloid plaques in Alzheimer's and diabetes: Novel leads for inhibitors

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When proteins change their structure and clump together, formation of amyloid fibrils and plaques may occur.

A team of scientists from the Technical University of Munich headed by Professor Aphrodite Kapurniotu have now developed molecules that suppress protein aggregation and could pave the way for new treatments to combat Alzheimer’s, type 2 diabetes and other cell-degenerative diseases.

The scientists designed and studied 16 different peptide molecules in order to find out which of them are able to impede the ‘clumping’ of the proteins amyloid beta and islet amyloid polypeptide, which are associated with Alzheimer’s and type 2 diabetes.

The researchers selected short sequences of the IAPP protein that correspond to the key regions involved in the interaction with the Alzheimer’s protein. Powerful inhibitors block pathologically relevant amyloid proteins in Alzheimer’s and diabetes.

The work performed by Professor Kapurniotu’s Peptide Biochemistry team at the TUM School of Life Sciences Weihenstephan together with researchers led by Professor Bernd Reif, TUM Department of Chemistry, and Professor Gerhard Rammes at Department of Anesthesiology, TUM Klinikum Rechts der Isar, identified among the designed molecules a number of powerful inhibitors of protein clumping.

The results reveal a novel class of peptide leads that block misfolding and clumping of pathologically relevant amyloid proteins in Alzheimer’s disease and type 2 diabetes, which could, in principle, be suitable for the development of therapeutics.


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Post Author: Carla Parsons

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