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Chemical Insights to Peptide Helix-Sheet-Nanofibre Equilibria (2005–2007)

Abstract:
Conversion of soluble proteins to insoluble amyloid aggregates is associated with >20 diseases (Alzheimers Huntingtons Parkinsons TypeII diabetes prion disorders). This phase transition is difficult to study and poorly understood but thought to proceed via beta sheets through protein mis-folding. We have developed a novel strategy to study helix-sheet-aggregate equilibria. By arraying multiple peptides on designed templates we can pre-organize peptide assemblies and control peptide folding aggregation composition and solubility of resulting nanofibres. Studying the formation and properties of these novel biopolymers will increase our understanding of amyloids while presenting new opportunities to develop unique biomaterials
Grant type:
ARC Discovery Projects
Researchers:

  • Professor David Fairlie

    NHMRC Leadership Fellow and Group L
    Institute for Molecular Bioscience
    NHMRC Leadership Fellow and Group L
    Institute for Molecular Bioscience
    Affiliate of ARC COE for Innovation
    ARC Centre of Excellence for Innovations in Peptide and Protein Science
    Institute for Molecular Bioscience
    of Institute for Molecular Bioscien
    Institute for Molecular Bioscience

  • Dr Philip Sharpe

    Lecturer
    School of Chemistry and Molecular Biosciences
    Faculty of Science
Funded by:
Australian Research Council