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Ember lab acquisition12/17/2023 These amyloidogenic proteins coalesce to form a cross β-sheet fibrils, which are observed as deposits in the brain. Some of the most well-characterized amyloids are composed of amyloid-β (Aβ), tau or α-synuclein (α-Syn) proteins and associate with cell death and brain dysfunction in Alzheimer’s (AD) and Parkinson’s disease (PD), the most prevalent neurodegenerative diseases. Their stability and resistance to degradation implicates them in: 1) adhesion and biofilm formation in bacteria 1, 2) spore development in fungi 2, 3) rubber biosynthesis in plants 3, 4) chemical catalysis 4, 5) materials 5, and 6) systemic organ amyloidosis and neurogenerative diseases in humans 6. In future studies, EMBER should enable high-throughput measurements of the fidelity of strain transmission in cellular and animal neurodegenerative diseases models, time course of amyloid strain propagation, and identification of pathogenic versus benign strains.Īmyloid fibrils are insoluble protein aggregates with a diverse range of biophysical properties, biological functions and association with human diseases. EMBER has in situ identified distinct conformational strains of tau inclusions in astrocytes, oligodendrocytes, and neurons from Pick’s disease. Our EMBER (excitation multiplexed bright emission recording) imaging method rapidly identifies conformational differences in Aβ and tau deposits from Down syndrome, sporadic and familial Alzheimer’s disease human brain slices. Here we use machine learning on the full information available in fluorescent excitation/emission spectra of amyloid binding dyes to identify six distinct different conformational strains in vitro, as well as Aβ deposits in different transgenic mouse models. However, there is a need to rapidly identify amyloid conformations in situ. In neurodegenerative diseases proteins fold into amyloid structures with distinct conformations (strains) that are characteristic of different diseases.
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