Effect of zinc binding on β-amyloid structure and dynamics: implications for Aβ aggregation.

@article{RezaeiGhaleh2011EffectOZ,
  title={Effect of zinc binding on β-amyloid structure and dynamics: implications for Aβ aggregation.},
  author={Nasrollah Rezaei-Ghaleh and Karin Giller and Stefan Becker and Markus Zweckstetter},
  journal={Biophysical journal},
  year={2011},
  volume={101 5},
  pages={1202-11}
}
Assembly of β-amyloid (Aβ) peptide into toxic oligomers is widely believed to initiate Alzheimer's disease pathogenesis. Under in vitro physiological conditions, zinc (Zn(II)) can bind to Aβ and redirect its assembly from amyloid fibrillar toward less toxic amorphous aggregation. Propensity of Aβ to go toward a specific form of aggregate state is determined by structural and dynamical properties of the initial monomeric as well as the aggregate state. Here we probe the structural and dynamical… CONTINUE READING
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