Alzheimer's disease research: unfolding the structure of β - amyloid fibrils

A neuroscience study carried out by a team of German scientists first reported the structure of β - amyloid fibrils isolated from the brain tissues of patients with Alzheimer's disease and cerebral amyloid vascular disease This result provides a new understanding of the structural basis of Alzheimer's disease and is also helpful for the development of related drugs The research was published in the British journal Nature communication on the 29th Alzheimer's disease is a kind of progressive neurodegenerative disease Because the pathogenesis is not clear, it is difficult to fundamentally prevent the progression of Alzheimer's disease At present, one of the characteristics of Alzheimer's disease is the deposition of β - amyloid fibrils in plaque and vascular wall Although the β - amyloid fibrils prepared in the laboratory have been well characterized in structure, the structure of these fibrils in the brain has been poorly understood This time, Markus van dridge and his colleagues, researchers from the University of Ulm in Germany, purified β - amyloid fibrils from the brain tissues of three Alzheimer's patients after their death, and analyzed their structures with frozen electron microscope In the three patients' samples, the research team found three different but structurally related forms of β - amyloid fibrils, and determined the molecular structure of one of them Unexpectedly, the structure of brain-derived fibrils is significantly different from that of β - amyloid fibrils For example, brain-derived β - amyloid fibrils are right-handed folded, and their peptide folding mode is also very different from that analyzed previously This structure highlights the importance of characterizing patient derived amyloid fibrils In addition, the study will help to understand the effect of mutations caused by Alzheimer's disease on β - amyloid protein, and will help to develop drugs to prevent the formation of such fibrils in the future.