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Membrane Charge Drives the Aggregation of TDP-43 Pathological Fragments.

Giacomo Corucci1, Devkee M Vadukul1, Nicolò Paracini2,3

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TDP-43 protein interactions with cell membranes are influenced by lipid charge. This finding may explain the spread of neurodegenerative diseases like ALS and Alzheimer's.

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Area of Science:

  • Neuroscience
  • Biophysics
  • Molecular Biology

Background:

  • TDP-43 protein is implicated in neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS), frontotemporal dementia, and Alzheimer disease.
  • TDP-43 normally functions in the nucleus and cytoplasm but is also found in extracellular vesicles, suggesting a role in intercellular communication.
  • Extracellular vesicles may facilitate the prion-like spread of misfolded TDP-43, contributing to disease progression.

Purpose of the Study:

  • To investigate the biophysical interactions between a TDP-43 fragment (M85) and synthetic phospholipid membranes.
  • To elucidate how lipid properties, specifically charge, influence TDP-43 binding and membrane disruption.

Main Methods:

  • Utilized a TDP-43 fragment (M85) and synthetic model phospholipid membranes.
  • Employed biophysical techniques including fluorescence, microscopy, and neutron reflectivity measurements.

Main Results:

  • Lipid charge significantly affects M85 interaction with membranes.
  • Increased negative lipid charge promotes M85 surface binding and protein aggregation.
  • Higher negative charge reduces the extent of lipid bilayer damage caused by M85.

Conclusions:

  • The interaction between M85 and lipid membranes is modulated by lipid charge.
  • These findings suggest a novel role for M85-lipid membrane interactions in the pathogenesis of TDP-43 proteinopathies.
  • Understanding these interactions could offer new therapeutic targets for neurodegenerative diseases.