Structural modification of NADPH oxidase activator (Noxa 1) by oxidative stress: An experimental and computational study

Pankaj Attri; Jae Hyun Park; Joey De Backer; Myeongkyu Kim; Ji Hye Yun; Yunseok Heo; Sylvia Dewilde; Masaharu Shiratani; Eun Ha Choi; Weontae Lee; Annemie Bogaerts

doi:10.1016/j.ijbiomac.2020.09.120

Structural modification of NADPH oxidase activator (Noxa 1) by oxidative stress: An experimental and computational study

Pankaj Attri, Jae Hyun Park, Joey De Backer, Myeongkyu Kim, Ji Hye Yun, Yunseok Heo, Sylvia Dewilde, Masaharu Shiratani, Eun Ha Choi, Weontae Lee, Annemie Bogaerts

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Abstract

NADPH oxidases 1 (NOX1) derived reactive oxygen species (ROS) play an important role in the progression of cancer through signaling pathways. Therefore, in this paper, we demonstrate the effect of cold atmospheric plasma (CAP) on the structural changes of Noxa1 SH3 protein, one of the regulatory subunits of NOX1. For this purpose, firstly we purified the Noxa1 SH3 protein and analyzed the structure using X-ray crystallography, and subsequently, we treated the protein with two types of CAP reactors such as pulsed dielectric barrier discharge (DBD) and Soft Jet for different time intervals. The structural deformation of Noxa1 SH3 protein was analyzed by various experimental methods (circular dichroism, fluorescence, and NMR spectroscopy) and by MD simulations. Additionally, we demonstrate the effect of CAP (DBD and Soft Jet) on the viability and expression of NOX1 in A375 cancer cells. Our results are useful to understand the structural modification/oxidation occur in protein due to reactive oxygen and nitrogen (RONS) species generated by CAP.

Original language	English
Pages (from-to)	2405-2414
Number of pages	10
Journal	International Journal of Biological Macromolecules
Volume	163
DOIs	https://doi.org/10.1016/j.ijbiomac.2020.09.120
Publication status	Published - 2020 Nov 15

Bibliographical note

Funding Information:
We gratefully acknowledge the European Marie Skłodowska-Curie Individual Fellowship “Anticancer-PAM” within Horizon 2020 (grant number 743546 ). This work was also supported by JSPS -KAKENHI grant number 20K14454 . Additionally, work was supported by several grants ( 2019M3A9F6021810 , NRF-2017M3A9F6029753 , NRF-2019M3E5D6063903 to W. Lee), Basic Science Research Program ( NRF-2016R1A6A3A04010213 to J.H. Yun) through the National Research Foundation of Korea and in part by the Brain Korea 21 (BK21) PLUS program (J.H.P.). EHC is thankful to National Research Foundation (NRF) of Korea, funded by the Korea government ( MSIT ) under the grant number ( NRF-2016K1A4A3914113 ). The computational work was carried out using the Turing HPC infrastructure at the CalcUA core facility of the Universiteit Antwerpen (UA), a division of the Flemish Supercomputer Center VSC, funded by the Hercules Foundation , the Flemish Government (department EWI) and the UA .

Funding Information:
We gratefully acknowledge the European Marie Sk?odowska-Curie Individual Fellowship ?Anticancer-PAM? within Horizon 2020 (grant number 743546). This work was also supported by JSPS-KAKENHI grant number 20K14454. Additionally, work was supported by several grants (2019M3A9F6021810, NRF-2017M3A9F6029753, NRF-2019M3E5D6063903 to W. Lee), Basic Science Research Program (NRF-2016R1A6A3A04010213 to J.H. Yun) through the National Research Foundation of Korea and in part by the Brain Korea 21 (BK21) PLUS program (J.H.P.). EHC is thankful to National Research Foundation (NRF) of Korea, funded by the Korea government (MSIT) under the grant number (NRF-2016K1A4A3914113). The computational work was carried out using the Turing HPC infrastructure at the CalcUA core facility of the Universiteit Antwerpen (UA), a division of the Flemish Supercomputer Center VSC, funded by the Hercules Foundation, the Flemish Government (department EWI) and the UA.

Publisher Copyright:
© 2020 Elsevier B.V.

All Science Journal Classification (ASJC) codes

Structural Biology
Biochemistry
Molecular Biology
Economics and Econometrics
Energy(all)

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This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.ijbiomac.2020.09.120

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Attri, P., Park, J. H., De Backer, J., Kim, M., Yun, J. H., Heo, Y., Dewilde, S., Shiratani, M., Choi, E. H., Lee, W., & Bogaerts, A. (2020). Structural modification of NADPH oxidase activator (Noxa 1) by oxidative stress: An experimental and computational study. International Journal of Biological Macromolecules, 163, 2405-2414. https://doi.org/10.1016/j.ijbiomac.2020.09.120

@article{883d0485d5aa4e3189e50df594c553ac,

title = "Structural modification of NADPH oxidase activator (Noxa 1) by oxidative stress: An experimental and computational study",

abstract = "NADPH oxidases 1 (NOX1) derived reactive oxygen species (ROS) play an important role in the progression of cancer through signaling pathways. Therefore, in this paper, we demonstrate the effect of cold atmospheric plasma (CAP) on the structural changes of Noxa1 SH3 protein, one of the regulatory subunits of NOX1. For this purpose, firstly we purified the Noxa1 SH3 protein and analyzed the structure using X-ray crystallography, and subsequently, we treated the protein with two types of CAP reactors such as pulsed dielectric barrier discharge (DBD) and Soft Jet for different time intervals. The structural deformation of Noxa1 SH3 protein was analyzed by various experimental methods (circular dichroism, fluorescence, and NMR spectroscopy) and by MD simulations. Additionally, we demonstrate the effect of CAP (DBD and Soft Jet) on the viability and expression of NOX1 in A375 cancer cells. Our results are useful to understand the structural modification/oxidation occur in protein due to reactive oxygen and nitrogen (RONS) species generated by CAP.",

author = "Pankaj Attri and Park, {Jae Hyun} and {De Backer}, Joey and Myeongkyu Kim and Yun, {Ji Hye} and Yunseok Heo and Sylvia Dewilde and Masaharu Shiratani and Choi, {Eun Ha} and Weontae Lee and Annemie Bogaerts",

note = "Funding Information: We gratefully acknowledge the European Marie Sk{\l}odowska-Curie Individual Fellowship “Anticancer-PAM” within Horizon 2020 (grant number 743546 ). This work was also supported by JSPS -KAKENHI grant number 20K14454 . Additionally, work was supported by several grants ( 2019M3A9F6021810 , NRF-2017M3A9F6029753 , NRF-2019M3E5D6063903 to W. Lee), Basic Science Research Program ( NRF-2016R1A6A3A04010213 to J.H. Yun) through the National Research Foundation of Korea and in part by the Brain Korea 21 (BK21) PLUS program (J.H.P.). EHC is thankful to National Research Foundation (NRF) of Korea, funded by the Korea government ( MSIT ) under the grant number ( NRF-2016K1A4A3914113 ). The computational work was carried out using the Turing HPC infrastructure at the CalcUA core facility of the Universiteit Antwerpen (UA), a division of the Flemish Supercomputer Center VSC, funded by the Hercules Foundation , the Flemish Government (department EWI) and the UA . Funding Information: We gratefully acknowledge the European Marie Sk?odowska-Curie Individual Fellowship ?Anticancer-PAM? within Horizon 2020 (grant number 743546). This work was also supported by JSPS-KAKENHI grant number 20K14454. Additionally, work was supported by several grants (2019M3A9F6021810, NRF-2017M3A9F6029753, NRF-2019M3E5D6063903 to W. Lee), Basic Science Research Program (NRF-2016R1A6A3A04010213 to J.H. Yun) through the National Research Foundation of Korea and in part by the Brain Korea 21 (BK21) PLUS program (J.H.P.). EHC is thankful to National Research Foundation (NRF) of Korea, funded by the Korea government (MSIT) under the grant number (NRF-2016K1A4A3914113). The computational work was carried out using the Turing HPC infrastructure at the CalcUA core facility of the Universiteit Antwerpen (UA), a division of the Flemish Supercomputer Center VSC, funded by the Hercules Foundation, the Flemish Government (department EWI) and the UA. Publisher Copyright: {\textcopyright} 2020 Elsevier B.V.",

year = "2020",

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day = "15",

doi = "10.1016/j.ijbiomac.2020.09.120",

language = "English",

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T1 - Structural modification of NADPH oxidase activator (Noxa 1) by oxidative stress

T2 - An experimental and computational study

AU - Attri, Pankaj

AU - Park, Jae Hyun

AU - De Backer, Joey

AU - Kim, Myeongkyu

AU - Yun, Ji Hye

AU - Heo, Yunseok

AU - Dewilde, Sylvia

AU - Shiratani, Masaharu

AU - Choi, Eun Ha

AU - Lee, Weontae

AU - Bogaerts, Annemie

N1 - Funding Information: We gratefully acknowledge the European Marie Skłodowska-Curie Individual Fellowship “Anticancer-PAM” within Horizon 2020 (grant number 743546 ). This work was also supported by JSPS -KAKENHI grant number 20K14454 . Additionally, work was supported by several grants ( 2019M3A9F6021810 , NRF-2017M3A9F6029753 , NRF-2019M3E5D6063903 to W. Lee), Basic Science Research Program ( NRF-2016R1A6A3A04010213 to J.H. Yun) through the National Research Foundation of Korea and in part by the Brain Korea 21 (BK21) PLUS program (J.H.P.). EHC is thankful to National Research Foundation (NRF) of Korea, funded by the Korea government ( MSIT ) under the grant number ( NRF-2016K1A4A3914113 ). The computational work was carried out using the Turing HPC infrastructure at the CalcUA core facility of the Universiteit Antwerpen (UA), a division of the Flemish Supercomputer Center VSC, funded by the Hercules Foundation , the Flemish Government (department EWI) and the UA . Funding Information: We gratefully acknowledge the European Marie Sk?odowska-Curie Individual Fellowship ?Anticancer-PAM? within Horizon 2020 (grant number 743546). This work was also supported by JSPS-KAKENHI grant number 20K14454. Additionally, work was supported by several grants (2019M3A9F6021810, NRF-2017M3A9F6029753, NRF-2019M3E5D6063903 to W. Lee), Basic Science Research Program (NRF-2016R1A6A3A04010213 to J.H. Yun) through the National Research Foundation of Korea and in part by the Brain Korea 21 (BK21) PLUS program (J.H.P.). EHC is thankful to National Research Foundation (NRF) of Korea, funded by the Korea government (MSIT) under the grant number (NRF-2016K1A4A3914113). The computational work was carried out using the Turing HPC infrastructure at the CalcUA core facility of the Universiteit Antwerpen (UA), a division of the Flemish Supercomputer Center VSC, funded by the Hercules Foundation, the Flemish Government (department EWI) and the UA. Publisher Copyright: © 2020 Elsevier B.V.

PY - 2020/11/15

Y1 - 2020/11/15

N2 - NADPH oxidases 1 (NOX1) derived reactive oxygen species (ROS) play an important role in the progression of cancer through signaling pathways. Therefore, in this paper, we demonstrate the effect of cold atmospheric plasma (CAP) on the structural changes of Noxa1 SH3 protein, one of the regulatory subunits of NOX1. For this purpose, firstly we purified the Noxa1 SH3 protein and analyzed the structure using X-ray crystallography, and subsequently, we treated the protein with two types of CAP reactors such as pulsed dielectric barrier discharge (DBD) and Soft Jet for different time intervals. The structural deformation of Noxa1 SH3 protein was analyzed by various experimental methods (circular dichroism, fluorescence, and NMR spectroscopy) and by MD simulations. Additionally, we demonstrate the effect of CAP (DBD and Soft Jet) on the viability and expression of NOX1 in A375 cancer cells. Our results are useful to understand the structural modification/oxidation occur in protein due to reactive oxygen and nitrogen (RONS) species generated by CAP.

AB - NADPH oxidases 1 (NOX1) derived reactive oxygen species (ROS) play an important role in the progression of cancer through signaling pathways. Therefore, in this paper, we demonstrate the effect of cold atmospheric plasma (CAP) on the structural changes of Noxa1 SH3 protein, one of the regulatory subunits of NOX1. For this purpose, firstly we purified the Noxa1 SH3 protein and analyzed the structure using X-ray crystallography, and subsequently, we treated the protein with two types of CAP reactors such as pulsed dielectric barrier discharge (DBD) and Soft Jet for different time intervals. The structural deformation of Noxa1 SH3 protein was analyzed by various experimental methods (circular dichroism, fluorescence, and NMR spectroscopy) and by MD simulations. Additionally, we demonstrate the effect of CAP (DBD and Soft Jet) on the viability and expression of NOX1 in A375 cancer cells. Our results are useful to understand the structural modification/oxidation occur in protein due to reactive oxygen and nitrogen (RONS) species generated by CAP.

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JO - International Journal of Biological Macromolecules

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Structural modification of NADPH oxidase activator (Noxa 1) by oxidative stress: An experimental and computational study

Abstract

Bibliographical note

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UN SDGs

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