Cold Atmospheric Plasma Modification of Amyloid β

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.