Cold Atmospheric Plasma Modification of Amyloid β
Cold atmospheric plasma (CAP) has attracted much attention in the fields of biotechnology and medicine owing to its potential utility in clinical applications. Recently accumulating evidence has demonstrated that CAP influences protein structures. However, there remain open questions regarding the m...
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| Format: | Article |
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MDPI AG
2021-03-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/22/6/3116 |
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| author | Maho Yagi-Utsumi Tomohiro Tanaka Yoko Otsubo Akira Yamashita Shinji Yoshimura Motohiro Nishida Koichi Kato |
| author_facet | Maho Yagi-Utsumi Tomohiro Tanaka Yoko Otsubo Akira Yamashita Shinji Yoshimura Motohiro Nishida Koichi Kato |
| author_sort | Maho Yagi-Utsumi |
| collection | DOAJ |
| description | Cold atmospheric plasma (CAP) has attracted much attention in the fields of biotechnology and medicine owing to its potential utility in clinical applications. Recently accumulating evidence has demonstrated that CAP influences protein structures. However, there remain open questions regarding the molecular mechanisms behind the CAP-induced structural perturbations of biomacromolecules. Here, we investigated the potential effects of CAP irradiation of amyloid β (Aβ), an amyloidogenic protein associated with Alzheimer’s disease. Using nuclear magnetic resonance spectroscopy, we observed gradual spectral changes in Aβ after a 10 s CAP pretreatment, which also suppressed its fibril formation, as revealed by thioflavin T assay. As per mass spectrometric analyses, these effects were attributed to selective oxidation of the methionine residue (Met) at position 35. Interestingly, this modification occurred when Aβ was dissolved into a pre-irradiated buffer, indicating that some reactive species oxidize the Met residue. Our results strongly suggest that the H<sub>2</sub>O<sub>2</sub> generated in the solution by CAP irradiation is responsible for Met oxidation, which inhibits Aβ amyloid formation. The findings of the present study provide fundamental insights into plasma biology, giving clues for developing novel applications of CAP. |
| first_indexed | 2024-03-10T13:06:51Z |
| format | Article |
| id | doaj.art-7db69b0111fc4bba9be61a1fa677d9ec |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T13:06:51Z |
| publishDate | 2021-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-7db69b0111fc4bba9be61a1fa677d9ec2023-11-21T11:03:18ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-03-01226311610.3390/ijms22063116Cold Atmospheric Plasma Modification of Amyloid βMaho Yagi-Utsumi0Tomohiro Tanaka1Yoko Otsubo2Akira Yamashita3Shinji Yoshimura4Motohiro Nishida5Koichi Kato6Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, Aichi 444-8787, JapanExploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, Aichi 444-8787, JapanDepartment of Plasmabio Science, Center for Novel Science Initiatives, National Institutes of Natural Sciences, Minato-ku, Tokyo 105-0001, JapanDepartment of Plasmabio Science, Center for Novel Science Initiatives, National Institutes of Natural Sciences, Minato-ku, Tokyo 105-0001, JapanDepartment of Plasmabio Science, Center for Novel Science Initiatives, National Institutes of Natural Sciences, Minato-ku, Tokyo 105-0001, JapanExploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, Aichi 444-8787, JapanExploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, Aichi 444-8787, JapanCold atmospheric plasma (CAP) has attracted much attention in the fields of biotechnology and medicine owing to its potential utility in clinical applications. Recently accumulating evidence has demonstrated that CAP influences protein structures. However, there remain open questions regarding the molecular mechanisms behind the CAP-induced structural perturbations of biomacromolecules. Here, we investigated the potential effects of CAP irradiation of amyloid β (Aβ), an amyloidogenic protein associated with Alzheimer’s disease. Using nuclear magnetic resonance spectroscopy, we observed gradual spectral changes in Aβ after a 10 s CAP pretreatment, which also suppressed its fibril formation, as revealed by thioflavin T assay. As per mass spectrometric analyses, these effects were attributed to selective oxidation of the methionine residue (Met) at position 35. Interestingly, this modification occurred when Aβ was dissolved into a pre-irradiated buffer, indicating that some reactive species oxidize the Met residue. Our results strongly suggest that the H<sub>2</sub>O<sub>2</sub> generated in the solution by CAP irradiation is responsible for Met oxidation, which inhibits Aβ amyloid formation. The findings of the present study provide fundamental insights into plasma biology, giving clues for developing novel applications of CAP.https://www.mdpi.com/1422-0067/22/6/3116amyloid βcold atmospheric plasmahydrogen peroxideNMR |
| spellingShingle | Maho Yagi-Utsumi Tomohiro Tanaka Yoko Otsubo Akira Yamashita Shinji Yoshimura Motohiro Nishida Koichi Kato Cold Atmospheric Plasma Modification of Amyloid β International Journal of Molecular Sciences amyloid β cold atmospheric plasma hydrogen peroxide NMR |
| title | Cold Atmospheric Plasma Modification of Amyloid β |
| title_full | Cold Atmospheric Plasma Modification of Amyloid β |
| title_fullStr | Cold Atmospheric Plasma Modification of Amyloid β |
| title_full_unstemmed | Cold Atmospheric Plasma Modification of Amyloid β |
| title_short | Cold Atmospheric Plasma Modification of Amyloid β |
| title_sort | cold atmospheric plasma modification of amyloid β |
| topic | amyloid β cold atmospheric plasma hydrogen peroxide NMR |
| url | https://www.mdpi.com/1422-0067/22/6/3116 |
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