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CAP 修饰来自嗜热细菌的模型蛋白的结构:CAP 介导失活的机制。

CAP modifies the structure of a model protein from thermophilic bacteria: mechanisms of CAP-mediated inactivation.

机构信息

Research Group PLASMANT, Department of Chemistry, University of Antwerp, Universiteitsplein 1, B-2610, Antwerp, Belgium.

Department of Biochemistry, College of Life Science & Biotechnology, Yonsei University, 134 Shinchon-Dong, Seodaemoon-Gu, Seoul, 120-749, Korea.

出版信息

Sci Rep. 2018 Jul 5;8(1):10218. doi: 10.1038/s41598-018-28600-w.

DOI:10.1038/s41598-018-28600-w
PMID:29977069
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6033864/
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.

摘要

冷等离体子体(CAP)在食品工业灭菌方面具有巨大潜力,可以使嗜热菌失活,但其中的机制尚不清楚。因此,我们在此研究 CAP 是否能够使嗜热菌的蛋白质变性/修饰。我们以产甲烷杆菌(Methanobacterium thermoautotrophicum)中的 MTH1880(MTH)作为模型蛋白,用空气介质阻挡放电(DBD)等离子体处理 10、15 和 20 分钟。我们使用圆二色性、荧光和 NMR 光谱分析以及 CAP 处理后的热变性和化学变性,研究 MTH 的结构变化。此外,我们还进行了分子动力学(MD)模拟,以确定天然和氧化蛋白的稳定性、灵活性和溶剂可及表面积(SASA)。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/778f/6033864/e94b78c91be8/41598_2018_28600_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/778f/6033864/6f1b6862c5fd/41598_2018_28600_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/778f/6033864/0eef0e29e379/41598_2018_28600_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/778f/6033864/c1f3d196390b/41598_2018_28600_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/778f/6033864/14f5ab317332/41598_2018_28600_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/778f/6033864/bd89efe8fa23/41598_2018_28600_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/778f/6033864/e94b78c91be8/41598_2018_28600_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/778f/6033864/6f1b6862c5fd/41598_2018_28600_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/778f/6033864/0eef0e29e379/41598_2018_28600_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/778f/6033864/c1f3d196390b/41598_2018_28600_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/778f/6033864/14f5ab317332/41598_2018_28600_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/778f/6033864/bd89efe8fa23/41598_2018_28600_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/778f/6033864/e94b78c91be8/41598_2018_28600_Fig6_HTML.jpg

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