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Cold Atmospheric Plasma Modification of Amyloid β.

Maho Yagi-Utsumi1,2, Tomohiro Tanaka1,3,4, Yoko Otsubo4,5,6

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Cold atmospheric plasma (CAP) prevents Alzheimer's-associated amyloid beta (Aβ) protein aggregation. CAP-generated hydrogen peroxide selectively oxidizes methionine, inhibiting Aβ fibril formation.

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NMRamyloid βcold atmospheric plasmahydrogen peroxide

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Area of Science:

  • Biotechnology
  • Plasma Medicine
  • Neuroscience

Background:

  • Cold atmospheric plasma (CAP) is recognized for its therapeutic potential in medicine and biotechnology.
  • Evidence suggests CAP can alter protein structures, but the precise molecular mechanisms are not fully understood.
  • Amyloid beta (Aβ) protein aggregation is central to Alzheimer's disease pathogenesis.

Purpose of the Study:

  • To investigate the effects of CAP on amyloid beta (Aβ) protein.
  • To elucidate the molecular mechanisms underlying CAP's influence on Aβ structure and function.
  • To explore CAP's potential for inhibiting Aβ fibril formation.

Main Methods:

  • Nuclear magnetic resonance (NMR) spectroscopy to observe Aβ structural changes.
  • Thioflavin T assay to monitor Aβ fibril formation.
  • Mass spectrometry to identify protein modifications.
  • Controlled exposure to cold atmospheric plasma (CAP) and pre-irradiated buffer solutions.

Main Results:

  • CAP pretreatment induced gradual spectral changes in Aβ.
  • CAP significantly suppressed Aβ fibril formation.
  • Mass spectrometry identified selective oxidation of methionine at position 35 (Met35) in Aβ.
  • Aβ dissolved in CAP-pre-irradiated buffer also showed Met35 oxidation, implicating reactive species.

Conclusions:

  • Hydrogen peroxide (H₂O₂) generated by CAP in solution is responsible for the oxidation of Aβ's Met35 residue.
  • Met35 oxidation by CAP-derived H₂O₂ effectively inhibits Aβ amyloid formation.
  • These findings offer insights into plasma biology and suggest novel applications for CAP in preventing protein aggregation diseases like Alzheimer's.