
%0 Journal Article
%A Lau, Tong-Lay 
%A Barnham, Kevin J. 
%A Curtain, Cyril C. 
%A Masters, Colin L. 
%A Separovic, Frances 
%T Magnetic Resonance Studies of &#946;-Amyloid Peptides
%J Australian Journal of Chemistry
%D 2003/05/23
%V 56
%N 5
%P 349-356
%K 
%R https://doi.org/10.1071/CH02268
%U https://www.publish.csiro.au/paper/CH02268 
%X The deposition of senile plaques is a characteristic event in the progression of Alzheimer&#39;s disease (AD). Associated with the progression of the disease, the main component of the deposited material, the &#946;-amyloid peptide (A&#946;), undergoes a structural transition and a toxic gain of function. For this reason, extensive structural studies of A&#946; and A&#946; fragments have been carried out in order to determine the relationship between neurotoxicity and conformational changes of the peptide that lead to fibril formation. NMR studies in aqueous solution and in membrane-mimicking environments are reviewed, and include the effects of temperature, pH, and metal ions on A&#946; structure. In addition, electron paramagnetic resonance (EPR) studies of A&#946; in model membranes and the effect of metals of A&#946; are discussed and demonstrate the pleiomorphic nature of the peptide. The contradictory results obtained from the various experiments are a result of studying different fragments of A&#946; and illustrate the importance of studying the full-length peptide. 
