CAP modifies the structure of a model protein from thermophilic bacteria: mechanisms of CAP-mediated inactivation
Abstract Cold atmospheric plasma (CAP) has great potential for sterilization in the food industry, by deactivation of thermophilic bacteria, but the underlying mechanisms are largely unknown. Therefore, we investigate here whether CAP is able to denature/modify protein from thermophilic bacteria. We...
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2018-07-01
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doaj-6557944bd4654ca4a25f449f93ce0eac2020-12-08T04:29:12ZengNature Publishing GroupScientific Reports2045-23222018-07-018111010.1038/s41598-018-28600-wCAP modifies the structure of a model protein from thermophilic bacteria: mechanisms of CAP-mediated inactivationPankaj Attri0Jeongmin Han1Sooho Choi2Eun Ha Choi3Annemie Bogaerts4Weontae Lee5Research Group PLASMANT, Department of Chemistry, University of AntwerpDepartment of Biochemistry, College of Life Science & Biotechnology, Yonsei UniversityDepartment of Biochemistry, College of Life Science & Biotechnology, Yonsei UniversityDepartment of Electrical and Biological Physics, Kwangwoon UniversityResearch Group PLASMANT, Department of Chemistry, University of AntwerpDepartment of Biochemistry, College of Life Science & Biotechnology, Yonsei UniversityAbstract Cold atmospheric plasma (CAP) has great potential for sterilization in the food industry, by deactivation of thermophilic bacteria, but the underlying mechanisms are largely unknown. Therefore, we investigate here whether CAP is able to denature/modify protein from thermophilic bacteria. We focus on MTH1880 (MTH) from Methanobacterium thermoautotrophicum as model protein, which we treated with dielectric barrier discharge (DBD) plasma operating in air for 10, 15 and 20 mins. We analysed the structural changes of MTH using circular dichroism, fluorescence and NMR spectroscopy, as well as the thermal and chemical denaturation, upon CAP treatment. Additionally, we performed molecular dynamics (MD) simulations to determine the stability, flexibility and solvent accessible surface area (SASA) of both the native and oxidised protein.https://doi.org/10.1038/s41598-018-28600-w |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Pankaj Attri Jeongmin Han Sooho Choi Eun Ha Choi Annemie Bogaerts Weontae Lee |
spellingShingle |
Pankaj Attri Jeongmin Han Sooho Choi Eun Ha Choi Annemie Bogaerts Weontae Lee CAP modifies the structure of a model protein from thermophilic bacteria: mechanisms of CAP-mediated inactivation Scientific Reports |
author_facet |
Pankaj Attri Jeongmin Han Sooho Choi Eun Ha Choi Annemie Bogaerts Weontae Lee |
author_sort |
Pankaj Attri |
title |
CAP modifies the structure of a model protein from thermophilic bacteria: mechanisms of CAP-mediated inactivation |
title_short |
CAP modifies the structure of a model protein from thermophilic bacteria: mechanisms of CAP-mediated inactivation |
title_full |
CAP modifies the structure of a model protein from thermophilic bacteria: mechanisms of CAP-mediated inactivation |
title_fullStr |
CAP modifies the structure of a model protein from thermophilic bacteria: mechanisms of CAP-mediated inactivation |
title_full_unstemmed |
CAP modifies the structure of a model protein from thermophilic bacteria: mechanisms of CAP-mediated inactivation |
title_sort |
cap modifies the structure of a model protein from thermophilic bacteria: mechanisms of cap-mediated inactivation |
publisher |
Nature Publishing Group |
series |
Scientific Reports |
issn |
2045-2322 |
publishDate |
2018-07-01 |
description |
Abstract Cold atmospheric plasma (CAP) has great potential for sterilization in the food industry, by deactivation of thermophilic bacteria, but the underlying mechanisms are largely unknown. Therefore, we investigate here whether CAP is able to denature/modify protein from thermophilic bacteria. We focus on MTH1880 (MTH) from Methanobacterium thermoautotrophicum as model protein, which we treated with dielectric barrier discharge (DBD) plasma operating in air for 10, 15 and 20 mins. We analysed the structural changes of MTH using circular dichroism, fluorescence and NMR spectroscopy, as well as the thermal and chemical denaturation, upon CAP treatment. Additionally, we performed molecular dynamics (MD) simulations to determine the stability, flexibility and solvent accessible surface area (SASA) of both the native and oxidised protein. |
url |
https://doi.org/10.1038/s41598-018-28600-w |
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