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The Functional Amyloid Orb2A Binds to Lipid Membranes.

Maria A Soria1, Silvia A Cervantes1, Thalia H Bajakian1

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Drosophila Orb2A protein interacts with anionic lipid membranes via its N-terminus. This interaction, dependent on membrane charge and curvature, inhibits amyloid formation, potentially regulating memory in vivo.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Lipid membranes influence amyloid protein aggregation.
  • Orb2, a Drosophila protein, forms functional amyloids crucial for long-term memory.
  • The Orb2A isoform's unique N-terminus is vital for amyloid formation and memory.

Purpose of the Study:

  • To investigate the interaction between the Orb2A N-terminus and lipid membranes.
  • To determine the structural basis of this interaction.
  • To explore how lipid membranes affect Orb2A amyloid formation.

Main Methods:

  • Circular dichroism (CD) spectroscopy.
  • Site-directed spin labeling coupled with electron paramagnetic resonance (EPR).
  • Transmission electron microscopy (TEM).

Main Results:

  • Orb2A (amino acids 1-88) interacts with anionic lipid membranes through an amphipathic helix at its N-terminus.
  • This interaction is modulated by membrane charge and curvature.
  • Anionic small unilamellar vesicles inhibit Orb2A amyloid fibril formation.

Conclusions:

  • Orb2A's N-terminus mediates direct lipid membrane interactions.
  • Membrane properties, specifically anionic charge and curvature, regulate Orb2A's structural behavior.
  • Anionic membrane binding offers a potential in vivo mechanism to control Orb2A amyloid formation and, consequently, memory processes.