and conclusions Fasman et al. demonstrated that an aluminium-induced transition towards Î²-sheet conformers of AÎ² 42 could be reversed to random coil soluble forms of the peptide by the addition of sodium orthosilicate (Na 4 SiO4 ) and, crucially, that this effect was attributable to the tight binding of Al 3+ by SiO4â . Unfortunately this conclusion was not sup4 ported by their experiments. What they did show was that in a non-aqueous medium of 2,2,2 triï¬uoroethanol (TFE) the addition of Al (dissolved in TFE) induced a conformational change in AÎ² 42 from predominantly Î±-helix/random coil to one which included a signiï¬cant component of Î²-sheets. When an aqueous solution of Na4 SiO4 was subsequently added to the mixture of AÎ²42 /Al/TFE a partial reversal of the Î²-sheet transition was achieved at a SiO4â to Al ratio of 1.0. This effect 4 may, as the authors suggested, have been due to the titration of Al out of AÎ² 42 though none of the required control experiments were carried out to conï¬rm this. For example, we do not know if the observed effect was due to (i) the addition of water (from the addition of aqueous Na 4 SiO4 )
Journal of Alzheimer's Disease – IOS Press
Published: Jan 1, 2007
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