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Heteroaggregation of Wild-Type and ALS Mutant SOD1.

Chad M Dashnaw1, Mayte Gonzalez1, Alireza Abdolvahabi2

  • 1Department of Chemistry and Biochemistry, Baylor University, Waco, Texas 76706, United States.

ACS Chemical Neuroscience
|December 11, 2025
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Summary

Wild-type (WT) copper-zinc superoxide dismutase-1 (SOD1) influences mutant SOD1 aggregation in amyotrophic lateral sclerosis (ALS). WT SOD1 generally slows mutant fibril formation but increases stability, with exceptions like D90A SOD1.

Keywords:
amyotrophic lateral sclerosiscoppermotor neuron diseasesuperoxide dismutasezinc

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Protein Misfolding Diseases

Background:

  • Mutant copper-zinc superoxide dismutase-1 (SOD1) proteins are linked to amyotrophic lateral sclerosis (ALS) pathogenesis.
  • The synergistic toxicity of wild-type (WT) SOD1 with mutant SOD1 is not fully understood.
  • Interactions between WT and mutant SOD1 in various states may underlie toxicity.

Purpose of the Study:

  • To investigate the effect of WT SOD1 on the aggregation rates and stability of mutant SOD1.
  • To determine if WT SOD1 influences the diverse homofibrillization rates of mutant SOD1.
  • To assess the proximity and colocalization of WT and mutant SOD1 within heterofibrils.

Main Methods:

  • In vitro coaggregation assays of WT and mutant SOD1.
  • Analysis of fibril formation kinetics (nucleation and propagation).
  • Assessment of fibril thermostability and cross-linking mass spectrometry.

Main Results:

  • WT SOD1 generally slowed mutant SOD1 fibril nucleation and propagation while enhancing fibril thermostability.
  • The D90A SOD1 mutation was an exception, showing minimal impact from WT SOD1 on nucleation rates.
  • Cross-seeding and mass spectrometry indicated that WT and mutant SOD1 can coexist and colocalize within heterofibrils.

Conclusions:

  • WT SOD1 modulates mutant SOD1 aggregation, typically inhibiting fibril formation but increasing stability.
  • Heterofibril formation suggests a potential mechanism for WT SOD1's influence on mutant SOD1 toxicity in ALS.
  • The colocalization within heterofibrils provides structural insights into SOD1 interactions in ALS.