Metal Ions in the association of A fibrils Sample Clauses

Metal Ions in the association of A fibrils. The overall structure as well as the N-terminal region of A capable of metal-ion coordination within the A fibrillization, plays a critical role in the neurotoxicity of the fibril.38,48 The solubility and deposition of amyloid is affected by this binding, leading to either beneficial or toxic effects on neuron health, which depends on the concentration of metal ions.37,45,49-50 This leads to the question of what is the beneficial concentration of metal and when this amount is too high that becomes harmful. In vitro, metal ions have been shown to accelerate the rate of formation of the peptide, and modify the morphology.40,51 Cu (II) has been shown to bind to the A(1-40) fibril, which causes dissociation and formation of an aggregate structure.40,52 However, Zn(II) can bind to A(10-21), and form fibrils without forming aggregates.36 Several techniques have been used to investigate fibril formation with and without metal ions, but so far, no technique has been able to resolve the position of metals along the fibril. AFM has been used to determine the large scale structure of metal free, solution-grown A protofibrils, fibril intermediates, and mature fibers on hydrophilic surfaces.53 However, an in-depth study has not yet been conducted relating copper and zinc’s role in large-scale fibril structure, nor has copper or zinc’s location along the fibril been directly verified.54 Raman spectroscopy was recently used to demonstrate that the metal ions, Zn(II) and Cu(II), bind to the peptide via histidine residues.55 This result is confirmed by solid- state NMR38 and electron paramagnetic resonance (EPR) spectroscopy,56 where the results show that the binding of the metal ions occurs via the histidines. But, there still ambiguity if all the histidines are involved or not.20 Metal ions have shown to bind to A in different sites, depending on the length of the A, and the specific sequence. For A(1-40), different groups have proposed that the binding occurs through histidine38,57 and possibly through tyrosine.48 However, other models have shown that tyrosine does not affect the metal binding while histidines 6, 13, and 14 are involved in the metal binding.40 Solid state NMR studies have suggested that the binding of metal ions is through histidines 13 and 14 for the whole peptide.44
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