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Immature ALS-associated mutant superoxide dismutases form variable aggregate structures through distinct

Harmeen K Deol1, Helen R Broom1, Bruna Siebeneichler1

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Mutant copper-zinc superoxide dismutase (SOD1) aggregation in amyotrophic lateral sclerosis (ALS) occurs via multiple pathways, not solely protein unfolding. Different mutations lead to distinct aggregate structures, impacting disease mechanisms.

Keywords:
ALSAggregate polymorphismAggregate structureAggregation mechanismProtein aggregationSOD1

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Protein misfolding and aggregation are central to neurodegenerative diseases like amyotrophic lateral sclerosis (ALS).
  • Mutant copper-zinc superoxide dismutase (SOD1) is a key factor in familial ALS pathogenesis.
  • The stability of the unmetallated, disulfide-reduced monomer (apoSH SOD1) is significantly affected by ALS-associated mutations.

Purpose of the Study:

  • To investigate the relationship between protein unfolding and aggregation propensity in mutant SOD1.
  • To characterize the different aggregation pathways and structures formed by mutant SOD1.
  • To explore the implications of these findings for understanding ALS mechanisms and protein aggregation in biotechnology.

Main Methods:

  • Light scattering and atomic force microscopy were used to analyze aggregate formation and morphology.
  • Attenuated total reflectance-Fourier transform infrared spectroscopy assessed protein secondary structure.
  • Thioflavin T binding assays quantified aggregate formation.

Main Results:

  • Aggregation of apoSH SOD1 was found to be poorly correlated with the extent of protein unfolding.
  • Two distinct aggregation behaviors were observed: high aggregators formed small assemblies, while low aggregators formed fiber-like structures.
  • Aggregates retained native-like anti-parallel beta sheet structure, irrespective of mutation or aggregation pathway.

Conclusions:

  • ALS-associated mutations promote apoSH SOD1 aggregation through multiple, distinct pathways.
  • The degree of unfolding does not directly predict aggregation propensity or structure.
  • These findings offer new insights into protein self-association in disease and potential biotechnological applications.