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Impact of Reactive Oxygen and Nitrogen Species Produced by Plasma on Mdm2-p53 Complex
Pankaj Attri1,2, Hirofumi Kurita3, Kazunori Koga4,5
1Center of Plasma Nano-Interface Engineering, Kyushu University, Fukuoka 819-0395, Japan.
Abstract:
The study of protein-protein interactions is of great interest. Several early studies focused on the murine double minute 2 (Mdm2)-tumor suppressor protein p53 interactions. However, the effect of plasma treatment on Mdm2 and p53 is still absent from the literature. This study investigated the structural changes in Mdm2, p53, and the Mdm2-p53 complex before and after possible plasma oxidation through molecular dynamic (MD) simulations. MD calculation revealed that the oxidized Mdm2 bounded or unbounded showed high flexibility that might increase the availability of tumor suppressor protein p53 in plasma-treated cells. This study provides insight into Mdm2 and p53 for a better understanding of plasma oncology.
Insights
Plasma treatment may enhance tumor suppressor protein p53 availability by increasing the flexibility of murine double minute 2 (Mdm2). This study offers insights into Mdm2-p53 interactions for plasma oncology.
Area of Science:
- Biochemistry and Molecular Biology
- Plasma Physics and Chemistry
- Cancer Research
Background:
- Protein-protein interactions, particularly between murine double minute 2 (Mdm2) and tumor suppressor protein p53, are crucial in cellular regulation.
- The impact of plasma treatment on these key protein interactions remains largely unexplored in scientific literature.
Purpose of the Study:
- To investigate the structural alterations in Mdm2, p53, and the Mdm2-p53 complex following plasma oxidation.
- To elucidate the potential effects of plasma treatment on Mdm2-p53 interactions and subsequent cellular consequences.
Main Methods:
- Utilizing molecular dynamic (MD) simulations to model and analyze structural changes.
- Comparing protein structures before and after simulated plasma oxidation.
Main Results:
- Molecular dynamic simulations indicated increased flexibility in both bounded and unbounded oxidized Mdm2.
- This enhanced Mdm2 flexibility suggests a potential increase in the availability of tumor suppressor protein p53 in cells exposed to plasma.
Conclusions:
- The study provides novel insights into the structural dynamics of Mdm2 and p53 under plasma conditions.
- Findings contribute to a better understanding of plasma oncology and its molecular mechanisms.
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