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Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One &#945;-Synuclein Monomer at a Time
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O-GlcNAc Modification of α-Synuclein Can Alter Monomer Dynamics to Control Aggregation Kinetics.

Kasun Gamage1, Binyou Wang2, Eldon R Hard2

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|July 31, 2024
PubMed
Summary

Posttranslational modifications, like O-GlcNAcylation, impact alpha-Synuclein aggregation differently. Glycosylation at T72 slows aggregation, while S87 may accelerate early stages, showing modifications don't uniformly affect protein clumping in neurodegenerative diseases.

Keywords:
Parkinson’s diseaseaggregationglycosylationintramolecular diffusionposttranslational modificationα-Synuclein

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Alpha-Synuclein (α-Syn) aggregation is central to Parkinson's disease pathogenesis.
  • Posttranslational modifications (PTMs) influence α-Syn aggregation kinetics.
  • O-GlcNAcylation of α-Syn has been reported to inhibit its aggregation.

Purpose of the Study:

  • To investigate the monomer dynamics of O-GlcNAcylated α-Synuclein at T72 and S87.
  • To correlate these dynamics with aggregation kinetics.
  • To understand how specific PTMs affect α-Syn aggregation propensity.

Main Methods:

  • Molecular dynamics simulations of unmodified, α-Syn(gT72), and α-Syn(gS87).
  • Analysis of protein compactness and diffusion.
  • Thioflavin T (ThT) fluorescence measurements to monitor fibril formation.

Main Results:

  • Glycosylation at T72 increased α-Syn monomer diffusion and decreased compactness.
  • Glycosylation at S87 decreased α-Syn monomer diffusion and increased compactness.
  • ThT assays confirmed slower aggregation for α-Syn(gT72) compared to unmodified α-Syn.
  • S87 modification predicted faster early aggregation, though not fully reflected in later-stage ThT kinetics.

Conclusions:

  • Posttranslational modifications exert non-uniform effects on α-Syn aggregation.
  • Monomer dynamics are crucial in determining aggregation propensity.
  • PTMs can differentially modulate the risk of α-Syn aggregation in neurodegenerative diseases.