The self-assembly of peptides into fibrils is commonly observed. Such fibrils may have biological roles and may also be useful in nanotechnology applications, as scaffolds to create metal nanowires or to template the self-assembly of other inorganic materials, for biosensors or as supports for cell adhesion. The misfolding of proteins into so-called amyloid fibrils is also implicated in amyloid diseases such as Alzheimer’s and type II diabetes. It has been suggested that amyloid fibrils are a generic state, although fibril structure and aggregation rate do depend on peptide sequence.
Prof. Ian Hamley, The Head of Physical Chemistry at the University of Reading and a Diamond Professor, and his team used Diamond to further their studies into the cause of diseases such as Alzheimer’s and CJD.
Insights were obtained into the secondary structure of the peptide studied. The peptides also showed pH responsiveness as well as liquid crystal phase formation at high concentration. These have potential applications in the design of novel polymer/peptide hybrid materials.
“One of the main contributing causes of Alzheimer’s disease and CJD is thought to be the formation of hard, insoluble plaques between the neurons in the brain. Diamond’s beamline for circular dichroism allows the investigation of the structure of the short peptides – an essential step in our research; without knowing the structure of the synthesised protein fragments, we cannot determine how they function.”
Prof Ian Hamley, Diamond Light Source
J.W. Hamley, V. Castelletto, C.M. Moulton, D. Myatt, G. Siligardi, C.L.P. Oliveira, J. Skow Pederson, I. Abutbul, D. Danino, Self-Assembly of a modified amyloid peptide fragment: pH responsiveness and nematic phase formation, Macromolecular Bioscience (2010) 10, 40-48.
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