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    Home > Biochemistry News > Biotechnology News > Cryo-electron microscopy structure of human brain amyloid β42 filaments

    Cryo-electron microscopy structure of human brain amyloid β42 filaments

    • Last Update: 2022-01-22
    • Source: Internet
    • Author: User
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    High-resolution observation of human Aβ42 fibrils

    Alzheimer's disease is characterized by loss of memory and other cognitive functions and the filamentous assembly of Aβ and tau in the brain
    Assembly of Aβ peptides into filaments ending at residue 42 is a central event
    Electron cryo-electron microscopy was used to determine the structure of Aβ42 filaments in the human brain (see perspectives by Willem and Föndrich)

    They identified two related S-type filaments, each composed of two identical protofilaments
    These structures will facilitate the development of better in vitro and animal models, inhibitors of Aβ42 assembly, and imaging agents with higher specificity and sensitivity


    Fiber assembly at the ends of amyloid beta peptide (Aβ42) is a central event in Alzheimer's disease
    Here, we report the cryo-electron microscopy (cryo-EM) structure of Aβ42 filaments from human brain
    Two structurally related S-shaped protofilament folds give rise to two types of filaments
    Type I filaments are mainly found in the brains of patients with sporadic Alzheimer's disease, and type II filaments are found in the brains of patients with familial Alzheimer's disease and other diseases
    The structure of Aβ42 microfilaments in the brain is different from that of microfilaments assembled in vitro
    In contrast, inapplicationNL-F CorporationIn mice, Aβ42 deposits consist of type II fibers
    Knowledge of human brain Aβ42 fiber structure may lead to the development of assembly inhibitors and improved imaging agents

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