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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

Experts

Professor David Fairlie

Centre Director of The Centre for C
Centre for Chemistry and Drug Discovery
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
Centre Director of Institute for Mo
Institute for Molecular Bioscience
NHMRC Leadership Fellow and Group L
Institute for Molecular Bioscience
David Fairlie
David Fairlie

Dr Philip Sharpe

Lecturer
School of Chemistry and Molecular Biosciences
Faculty of Science
Philip Sharpe
Philip Sharpe