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    More effective treatment of Alzheimer’s

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    Developing effective treatments for Alzheimer’s disease has proven difficult. The most effective ones that have just been approved provide little effect. There are several main reasons why they are not effective, one of which is that the antibodies used do not bind to all types of toxic aggregates that cause Alzheimer’s disease.

    In Alzheimer’s disease, amyloid beta protein begins to form aggregates. This process is called aggregation, and the clamp created is called aggregation. Researchers have previously shown that treatment with the peptide somatostatin begins to break down aggregate components into the body. In a new study, researchers are using antibodies that can bind to toxic aggregate and prevent it from harming cells.

    Small chunks may be more toxic

    The problem with the treatments currently being tested in patient studies is that the antibody binds much more strongly to the large mass and very little to the small mass. Small chunks are as toxic as large chunks, and many consider them even more dangerous in practice because they can move more.

    The purpose of the current study was to develop an antibody format that could bind to both large and small amyloid beta masses. Antibodies use the avidity effect to bind strongly to the target. This requires both arms of the antibody to bind to the same target at the same time (see figure).

    The distance between the antibody arms is important for how small the aggregates that the antibody can bind strongly to. If the aggregates are less than the distance between the arms, they will not bond tightly to the aggregates. If it is large, they bind very strongly to the aggregate. In a new article, researchers have developed a new antibody format that binds to small aggregates with a short distance between the arms. The new format also has more binding sites to make the bond stronger.

    “Thanks to the avidity effect, the new antibody format is at least 40 times stronger at binding to aggregates. The new type of antibody can also bind to small aggregates with avidity not found in other antibodies. That’s great, “said Greta Hartkovist, senior lecturer and associate professor of protein drug design at Uppsala University, who led the study.

    Effect of antibody Tested in cell culture experiments, it has been shown that a new antibody format can save cells from death caused by amyloid beta aggregates. Preclinical studies were not included, but the team believes their results suggest that new antibody designs may be more effective than those tried so far. ..

    “Although the focus of our research was to target the amyloid beta protein in Alzheimer’s disease, new antibody designs are common and can be applied to other disease-causing masses. From a long-term perspective, new formats It opens up new avenues for future treatments not only in Alzheimer’s disease, but also in other diseases such as Parkinson’s disease where proteins begin to aggregate. ” A doctoral student in protein drug design and studying.

    The study was published in Translational neurodegeneration..


    New methods show potential treatment for Alzheimer’s disease


    For more information:
    Fadi Rofo et al, a new multivalent design of monoclonal antibodies, improves the binding strength of amyloid beta to soluble aggregates. Translational neurodegeneration (2021). DOI: 10.1186 / s40035-021-00258-x

    Provided by
    Uppsala University

    Quote: Https: //medicalxpress.com/news/2021-09-effective-treatment-more effective treatment for Alzheimer’s disease (September 28, 2021) obtained on September 28, 2021 from alzheimer.html

    This document is subject to copyright. No part may be reproduced without written permission, except for fair transactions for personal investigation or research purposes. The content is provided for informational purposes only.

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    The post More effective treatment of Alzheimer’s appeared first on California News Times.

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