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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Main Authors: Pankaj Attri, Jeongmin Han, Sooho Choi, Eun Ha Choi, Annemie Bogaerts, Weontae Lee
Format: Article
Language:English
Published: Nature Publishing Group 2018-07-01
Series:Scientific Reports
Online Access:https://doi.org/10.1038/s41598-018-28600-w
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spelling 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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