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    Characterising Interactions Between Amyloid-beta 42 and Amylin Peptide Heterodimers: A Molecular Simulation Approach

    Access Status
    Fulltext not available
    Embargo Lift Date
    2025-07-19
    Authors
    Sonar, Krushna Satish
    Date
    2022
    Supervisor
    Ricardo Mancera
    Prashant Bharadwaj
    Type
    Thesis
    Award
    PhD
    
    Metadata
    Show full item record
    Faculty
    Health Sciences
    School
    Curtin Medical School
    URI
    http://hdl.handle.net/20.500.11937/92792
    Collection
    • Curtin Theses
    Abstract

    Amyloid-beta 42 (Aß42) and amylin are intrinsically disordered peptides. Pathogenic aggregation of peptides results in Alzheimer’s disease (AD) and Type-2 diabetes (T2D), by Aß42 and amylin, respectively. High risk of AD in T2D patients exists due to cross-aggregation in brain. Difficulty in in-vitro characterisation aggregation mechanism elusive. We have managed to shed light on mechanism by sampling conformations and exploiting the hydrophobic nature of peptides using enhanced simulation on monomer (Aß42), Aß42 homo-and heterodimer (Aß42-Amylin).

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