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Aggregation rates of amyloid beta increase dramatically in acidic vesicles

last modified May 27, 2014 02:27 PM
New research by the Laser Analytics Group sheds light on the protein aggregation reactions at the heart of Alzheimer's disease.

Research led by Dr. Gabi Kaminski Schierle, and recently published in Chemistry and Biology, reveals how Amyloid-β, a protein involved in Alzheimer's disease, develops into a pathogenic species. The group has developed a fluorescent sensor concept,  which makes it  possible to study how proteins misfold and aggregate in living cells. Crucially it was shown that the kinetics of Aβ aggregation are vastly different in brain cells, than in the test tube, and further that  the most pathogenic forms of Amyloid-β aggregate much faster in live cells than had previously been assumed from corresponding studies in test tubes. The  technique makes it possible to correlate the appearance of certain aggregate species with their gain of toxic function thus providing a tool  to screen for potential therapeutic agents in  more efficient ways than hitherto possible.

Read more on this research in a press release on Alzforum.