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Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

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Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
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Membrane Phase, Charge, and Curvature Regulate α-Synuclein Binding Dynamics.

Orianna H Kou1, Cailyn M Sakurai2, Stephanie Y Ramirez3

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Alpha-synuclein (αSyn) binding to lipid membranes depends on membrane charge and phase. This study reveals how these factors, along with curvature, control αSyn

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Published on: May 30, 2021

Area of Science:

  • Biochemistry and Biophysics
  • Neuroscience
  • Molecular Biology

Background:

  • Alpha-synuclein (αSyn) is intrinsically disordered and interacts with lipid membranes.
  • These interactions are crucial for αSyn's function and its role in synucleopathies.
  • Previous studies examined membrane charge, phase, and curvature independently.

Purpose of the Study:

  • To investigate how membrane phase and charge jointly regulate αSyn binding.
  • To understand the combined effects on αSyn's curvature sensitivity and dynamic membrane association.
  • To resolve both equilibrium and kinetic contributions to protein-membrane binding.

Main Methods:

  • Systematic investigation using fluorescence microscopy and circular dichroism spectroscopy.
  • Utilized fluorescence recovery after photobleaching (FRAP) for dynamic measurements.
  • Complemented experimental data with coarse-grained molecular dynamics simulations.

Main Results:

  • αSyn preferentially binds curved gel-phase membranes under zwitterionic conditions.
  • Anionic lipids enhance αSyn binding to liquid-phase membranes but reduce it in gel-phase.
  • Membrane phase and charge influence the stability of membrane-associated αSyn, promoting kinetically stabilized states.
  • Simulations indicate curvature-induced defect formation is amplified in gel-phase membranes.

Conclusions:

  • αSyn-membrane interactions are governed by a cooperative interplay of membrane phase, curvature, and charge.
  • Both thermodynamic and kinetic aspects of protein-membrane binding are critical.
  • Findings provide insights into αSyn's role in synucleopathies.