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    Home > Active Ingredient News > Immunology News > Nature Sub-journal Depth Analysis! Mysterious link between Alzheimer's disease and diabetes!

    Nature Sub-journal Depth Analysis! Mysterious link between Alzheimer's disease and diabetes!

    • Last Update: 2020-07-19
    • Source: Internet
    • Author: User
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    , 26, 2020 /PRNewswire-bioon/ -- In a study published in the International Journal ofNature Structural and Molecular Biology, scientists from the Ulich Research Center in Germany have revealed the molecular association between Alzheimer's disease
    anddiabetes; For the first time in the study, researchers used cryogenic electron microscopy to obtain clear images of how individual molecules are arranged in protein chains that form typicaldiabetessediments, the structure of the protofibers that are very similar to those of the central fibers in Alzheimer's disease, and the relevant studies have found or are largely consistent with previous findingsPhoto Source: Forschungszentrum J?lich/HHU D?sseldorf/Gunnar Schr?der
    About 120 years ago, U.Sdoctor Eugene Lindsay Opie found unusual protein deposits in the pancreas of type 2diabetespatients, much like the deposits found in the brains of patients with a variety of neurodegenerative diseases, and type 2 diabetes, formerly known as adult diabetes, is made up of small protein harnesses called prolified fibrous, in the event of diabetesMade up of the peptide hormone I
    app
    , which in the pancreas promotes abnormal and even dead beta cells responsible for producing insulin, which plays an important role in helping the body lower blood sugar, explained gunnar Schroder, a researcher, who has been studying these amyloid fibers for years, but for a long time, researchers have been able to study them with lower resolutions In 2017, researchers worked together to develop the first-ever atomic-level 3-D model of the fiber, in which case they discovered an Alzheimer's fiber consisting of amyloid beta peptides (A-beta) For the first time, the researchers successfully reconstructed the 3D reconstruction of the IAPP fiber at a higher resolution (0.4 nm), and among other details, the precise arrangement of the molecules in the fibers became clear, revealing how individual I
    app molecules are stacked with each other and form fibers with An S-section, similar to S-folds in A-beta fibers, a typical feature of Alzheimer's disease The similarity is interesting, explains researcher Wolfgang Hoyer, that there is an epidemiological correlation between Alzheimer's disease and diabetes, where People with Alzheimer's tend to have a higher risk of diabetes, and vice versa, and perhaps other links, such as scientists being able to detect small impurities in typical "foreign" I
    app peptides in Alzheimer's patients, and researchers testing mice to test for a type of cellulose this high-resolution fiber model could provide a platform for researchers to study the formation of raw fibers in the event of diabetes, as well as to help develop drugs that directly address the cause, such as the development of new inhibitors to inhibit the formation of raw fibers, and researchers have studied binding proteins for many years, which inhibit the formation of amyloid proteins in a single molecule, which can slow or even block diabetes, Al Another approach is the development of alternatives to IAPP peptides, which are not easy to form in the form of primary fibers, and one of the functions that I
    app is to act as appetite suppressor stakes in the body, so this alternative is not only meaningful for the treatment of type 2 diabetes, but also for the treatment of obesity such as type 1 diabetes and disease frozen electron microscopy is still a relatively new research method that determines the structure of biomolecules at yard level, and researcher Jacques Dubochet and three others won the 2017 Nobel Prize in Chemistry for developing the technology Cryptoscope technology can accomplish tasks similar to long-standing methods such as X-ray crystallography and NMR spectroscopy (NUCLEAR magnetic resonance), in which in X-ray crystallography technologies, such as proteins, DNA, bacterial and viral molecules are first converted into crystalform, whereas in contrast to cryoscopic electronosis and NMR spectroscopy With the help of technology, researchers can analyze protein structure elements in a natural state, using cryoscopy technology as an example, where specimens are first dissolved into water, then quickly frozen, and then studied again with cryo-electronic microscopes, a method that may have a particular advantage when studying large structures hundreds or thousands of proteomics (BioValleyBioon.com) References: 1 R?der, C., Kupreichyk, T., Gremer, L et al Cryo-EM structure of islet polyloid polypeptide fibrils sauis with amyloid-beta fibrils Nat Struct Mol Biol (2020) (2) New oed o'r link from Alzheimer's and .
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