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    Home > Biochemistry News > Biotechnology News > Nature: The first detailed image of ALS-related molecules opens the door to treatment

    Nature: The first detailed image of ALS-related molecules opens the door to treatment

    • Last Update: 2021-12-28
    • Source: Internet
    • Author: User
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    Picture: The newly discovered massive TDP-43 structure comes from the brains of ALS patients


    Source: B.


    Scientists have determined for the first time the molecular structure related to amyotrophic lateral sclerosis (ALS) and a variety of other neurodegenerative diseases


    Amyotrophic lateral sclerosis is the most common motor neuron disease in adults.


    Although the cause of amyotrophic lateral sclerosis is unclear, it is known that abnormal accumulation of a protein called TDP-43 in nerve cells is a hallmark pathological feature of amyotrophic lateral sclerosis


    TDP-43 is found in healthy cells in our body, but in the brains of patients with these diseases, it gathers together to form "aggregates" in the brain


    Although scientists have been aware of this for some time, the potential for translating this information into treatments is still limited, because the molecular structure of TDP-43 aggregates is still unknown so far


    Now, the team of scientists from the MRC Molecular Biology Laboratory is collaborating with researchers from Tokyo Metropolitan Institute of Medicine and Aichi Medical University, Japan.


    The study, supported by the Medical Research Council and published in the journal Nature, found structural features that had not been discovered before, such as a filamentous double helix-like fold


    The structure of TDP-43 observed in human brain samples in this study is the same in samples from different regions of the two human brains, but it is different from what was seen in previous studies trying to reconstruct TDP-43 aggregates in test tubes


    Previously, it was thought that TDP-43 interacts similarly with similar proteins related to other neurodegenerative diseases (such as Alzheimer's disease)


    These unique structural features mean that TDP-43 may interact uniquely with diagnostic tools and drugs in the brain


    This research provides new possibilities for the development of compounds specifically targeting the structural features of TDP-43, including those responsible for aggregation


    Dr.


    "Now that we know the aggregate structure of TDP-43 and its uniqueness, we can use it to find better ways to diagnose diseases early


    "We are very pleased to be able to use this blueprint in the laboratory to begin identifying compounds that bind to the unique site of TDP-43, with the goal of identifying potential therapies for further research
    .

    "I want to especially thank the patients with amyotrophic lateral sclerosis and their families who donated their brains to research to help us better understand this terrible disease
    .
    "

    Dr.
    Joe Latimer, Director of Neuroscience and Mental Health of the British Medical Research Council, who funded the study, said: "These findings have important and urgent contributions to our understanding of amyotrophic lateral sclerosis and related neurodegenerative diseases
    .
    "Determining the structure of a known disease-causing protein is the first step in understanding its role in disease development
    .

    "At present, the cause of ALS is not yet clear, but understanding the structure of TDP-43 will redefine scientists' views on disease progression, enabling them to adopt new methods to develop treatments and diagnostics
    .
    "

    DOI

    10.
    1038 / s41586-021-04199-3

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