Study reveals beta-amyloid polymer structure that causes Alzheimer's disease development

"About 10 percent of Alzheimer's cases are caused by family mutations," said Wei Qiang, assistant professor of biophysical chemistry at Binghamton UniversityAnother 90% of cases were caused by improper folding of wild amyloid proteinWe need to understand the molecular basis of disease pathologySo we may one day be able to create drugs to prevent the degeneration of the diseaseAlzheimer's disease is developed by a chain structure called profibre, which appears in brain cells and kills brain cellsResearchers at Qiang and the University of Colorado and Denver used high-resolution solid-state magnetic resonance spectra to study the fibersTheir work revealed that these fibers may have major variations in the molecular structure of amyloid deposition in the human brainWhat's more, fiber can serve as a "seed" for further fiber deposition, a potential lying factor for Alzheimer's disease" this work describes a molecular structure model of a pathologically associated beta-amyloid fiber variant," Qiang said"We have shown that this mutation may lead to rapid seeding of new amyloid protein fibers, which may help to spread and amplify amyloid deposition in the human brainQiang and his team are studying several other types of fiber variants, in particular the correlation between structural variation, their seeding capacity, and the resulting cytotoxicity levels"We have achieved exciting results and a new manuscript describing these further discoveries is being prepared," Qiang saidReferences:Zhi-Wen Hu et al, Molecular structure of n-terminal pholated beta-amyloid fibril, Proceedings of the National Academy of Sciences (2019)DOI: 10.1073/pnas.181853016Original title: PNAS: Study Reveals beta-amyloid protein aggregate structure, reveals the development of Alzheimer's disease