Synthetic peptides may suppress formation of harmful amyloid aggregates

Munich [Germany], November 9 (ANI): In Alzheimer's disease, toxic protein clumps and deposits known as amyloid plaques are connected to the death of brain cells. Similar pathways are crucial in type 2 diabetes as well. The Technical University of Munich is leading the development of "mini-proteins," or peptides, that can bind the proteins that make amyloids and stop them from aggregating into deadly amyloids.
The development of harmful protein aggregates that lead to cell death is a known cause of numerous cell-and neurological disorders. Type 2 diabetes mellitus and Alzheimer's disease, which have more than 50 million and 400 million individuals globally, respectively, are prominent examples of these disorders. Importantly, as the population ages, the number of people with diabetes and Alzheimer's disease continuously increases. The two illnesses are still incurable, though. New therapeutic strategies are thus desperately needed.
A promising strategy is to stop the production of toxic amyloid aggregates. Aphrodite Kapurniotu, a professor of Peptide Biochemistry at the Technical University of Munich (TUM), and her colleagues have created unique synthetic peptides that can inhibit the hazardous amyloid aggregation associated with both disorders in experimental settings.
Type 2 diabetes and Alzheimer's disease interact molecularly.
Previous research demonstrated that specific "cross-interactions" between the two illnesses' amyloidogenic proteins significantly accelerated the amyloid aggregation process. These results may help to explain why individuals with one of the two diseases may also be at a higher risk for the other disease.
The team developed synthetic peptides that could function as effective inhibitors of amyloid aggregation in both diseases. Prof. Kapurniotu says: "The designed peptides are in fact able to bind the amyloidogenic proteins linked to both diseases and to effectively suppress both cytotoxic amyloid aggregation and amyloid cross-accelerating interactions. Remarkably, although the mixed aggregates formed by interactions of the designed peptides with the amyloidogenic proteins look very similar to harmful amyloid aggregates, they are completely devoid of cytotoxic effects. Moreover, these amyloid-resembling mixed aggregates become more efficiently taken up by the phagocytic immune cells than amyloid aggregates."
Future research will open the door to medical applications.
There is mounting evidence that type 2 diabetes and Alzheimer's disease are related. Thus, according to Prof. Kapurniotu, the developed peptides may make excellent candidates for the creation of medications to treat both diseases. (ANI)