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Local Ionic Conditions Modulate the Aggregation Propensity and Influence the Structural Polymorphism of α-Synuclein.

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Summary
This summary is machine-generated.

Physiologically relevant ions like calcium (Ca2+) and sodium (Na+) accelerate alpha-synuclein (aSyn) aggregation, a key process in Parkinson's disease (PD). Ion concentration influences aSyn structure and fibril formation, offering insights into PD mechanisms.

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Structural Biology

Background:

  • Parkinson's disease (PD) is characterized by alpha-synuclein (aSyn) aggregation.
  • The exact triggers and mechanisms of aSyn aggregation are not fully understood.
  • Local environmental factors, including ion concentrations, may influence aSyn aggregation.

Purpose of the Study:

  • To investigate the impact of physiologically relevant ions (Ca2+ and Na+) on aSyn aggregation.
  • To explore how these ions affect aSyn monomer structure, dynamics, and fibril polymorphism.

Main Methods:

  • Thioflavin T (ThT) fluorescence assays for aggregation kinetics.
  • Nuclear Magnetic Resonance (NMR) spectroscopy (1H-15N HSQC) for structural dynamics.
  • Small-angle neutron scattering (SANS) and hydrogen-deuterium exchange mass spectrometry (HDX-MS) for structural changes.
  • Molecular dynamics (MD) simulations for atomic-level insights.
  • Atomic force microscopy (AFM) for fibril morphology.

Main Results:

  • All tested ions accelerated aSyn aggregation, with Ca2+ showing the most potent effect.
  • Ca2+ binds to the C-terminus, while Na+ interacts non-specifically.
  • Na+ promotes extended aSyn structures, Ca2+ induces moderate extension and alters solvent dynamics.
  • Distinct fibril polymorphs were observed under different ionic conditions.

Conclusions:

  • The local ionic environment significantly influences aSyn structure, dynamics, and aggregation propensity.
  • Ion-induced conformational changes and altered solvent interactions contribute to aSyn aggregation.
  • Findings provide molecular insights into PD pathogenesis and potential therapeutic targets.