UC SANTA BARBARA (US) — A new research method has potential for use in early diagnosis and eventual treatment of plaque-related diseases, like Alzheimer’s.
Using ion-mobility spectrometry-mass spectrometry (IMS-MS), scientists deduced peptide self-assembly and then examined a series of amyloid-forming peptides clipped from larger peptides or proteins associated with disease.
Understanding the fundamental forces that relate aggregation, shape, and biochemistry of soluble peptide aggregates is central to developing diagnostic and therapeutic strategies for amyloid diseases, says lead author Michael Bowers, professor of chemistry and biochemistry at University of California, Santa Barbara.
The work is published in the journal Nature Chemistry.
Amyloid diseases are characterized by plaque that aggregates into toxic agents that interact with cellular machinery, Bowers says. Amyloid plaques are protein fibrils that, in the case of Alzheimer’s disease, develop prior to the appearance of symptoms.
“The systems we use are model systems, but the results are groundbreaking,” says Bowers.
The new research provides the first examples of the conversion of randomly assembled aggregates of small peptides into ordered beta sheets that comprise fibrils, the final structural state of the aggregation process.
Other plaque-related diseases include Parkinson’s, Type 2 diabetes, and atherosclerosis.
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