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Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
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DNA-triggered aggregation of copper, zinc superoxide dismutase in the presence of ascorbate

Jun Yin1, Si Hu, Wei Jiang

  • 1Key Laboratory of Pesticide and Chemical Biology, Ministry of Education, and School of Chemistry, Central China Normal University, Wuhan, China.

Plos One
|September 3, 2010
PubMed

Insights

Oxidative damage to wild-type copper, zinc superoxide dismutase (SOD1) can lead to protein aggregation. DNA accelerates this oxidative aggregation by neutralizing positive charges on SOD1, revealing key molecular forces in protein aggregation.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Chemistry

Background:

  • The oxidative damage hypothesis suggests mutant and wild-type (WT) copper, zinc superoxide dismutase (SOD1) can cause cellular damage.
  • It remains unclear if SOD1 oxidative damage contributes to SOD1 aggregate formation.

Purpose of the Study:

  • To investigate the oxidative aggregation of WT SOD1 under neutral conditions with ascorbate (Asc) and DNA.
  • To understand the role of oxidation and DNA in SOD1 aggregation.

Main Methods:

  • Exposure of WT SOD1 to ascorbate and DNA under neutral conditions.
  • Analysis of SOD1 oxidation, DNA binding affinity, hydrophobicity, and aggregation.
  • Investigation of charge neutralization's role in aggregation.

Main Results:

  • WT SOD1 was oxidized by ascorbate.
  • Oxidized SOD1 exhibited increased affinity for DNA and enhanced aggregation.
  • DNA significantly accelerated SOD1 oxidative aggregation.
  • A correlation was found between oxidation, hydrophobicity, and aggregation, with DNA binding neutralizing positive charges.

Conclusions:

  • Oxidative damage to WT SOD1, particularly in the presence of DNA, promotes protein aggregation.
  • DNA binding, through charge neutralization, is a critical step in SOD1 oxidative aggregation.
  • This study elucidates molecular forces driving protein aggregation, relevant to SOD1-related diseases.

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