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Zinc Induced Aβ16 Aggregation Modeled by Molecular Dynamics.

Anna P Tolstova1, Alexander A Makarov1, Alexei A Adzhubei1

  • 1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov St. 32, 119991 Moscow, Russia.

International Journal of Molecular Sciences
|November 27, 2021
PubMed
Summary

Zinc binding to beta-amyloid 16-mers (Aβ16) promotes neurotoxic aggregate formation. Aβ16 dimers coordinated by zinc ions are key to this rapid aggregation process, influencing Alzheimer's disease pathology.

Keywords:
Aβ16MDaggregationbeta-amyloidmetal binding sitezinc ion

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Computational Biology

Background:

  • Zinc is known to influence beta-amyloid (Aβ) aggregation, contributing to neurotoxicity in Alzheimer's disease.
  • The precise mechanism by which zinc affects Aβ aggregation, particularly at the early stages, remains incompletely understood.

Purpose of the Study:

  • To investigate the mechanism of zinc-induced aggregation of Aβ16 peptides using molecular dynamics simulations.
  • To elucidate the role of zinc coordination in the formation of Aβ16 dimers and subsequent aggregate structures.

Main Methods:

  • Molecular dynamics simulations were employed to study Aβ16 aggregation in the presence and absence of zinc ions.
  • Analysis focused on the formation of Aβ16 dimers, zinc coordination within the 11EVHH14 site, and the kinetics of aggregate formation.

Main Results:

  • Zinc-induced formation of Aβ16 dimers, with zinc coordinated at the 11EVHH14 site, significantly accelerates aggregation compared to zinc-free systems.
  • The presence of pre-formed Aβ16 dimers is crucial for rapid aggregation; adding zinc to existing dimers has minimal impact.
  • Excessive zinc at early stages can hinder aggregation by occupying additional sites, leading to slower kinetics and smaller complexes.

Conclusions:

  • Zinc-mediated formation of Aβ16 dimers is a critical step in the generation of neurotoxic non-fibrillar beta-amyloid aggregates.
  • The optimal zinc concentration and coordination are essential for efficient aggregation, with specific dimer structures being energetically favorable.