Reactive species driven oxidative modifications of peptides—Tracing physical plasma liquid chemistry

Reactive species driven oxidative modifications of peptides—Tracing physical plasma liquid chemistry
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活性物质驱动的肽氧化修饰——追踪物理等离子体液体化学

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发表时间:
2021
期刊:
影响因子:
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通讯作者:
K. Wende
K. Wende
中科院分区:
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文献类型:
--
作者:
S. Wenske;J. Lackmann;Larissa M Busch;Sander Bekeschus;T. von Woedtke;K. Wende

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物理等离子体的出水包括大量的活性物质,这些活性物质可以与生物分子相互作用,产生与生理过程相当的化学修饰,例如翻译后蛋白质修饰(OxPTM)。因此,这项工作的目的是了解物理等离子体衍生的活性物种在引入蛋白质中oxPTM样修饰中的作用。一个由10个多肽组成的人工多肽文库被筛选,以抵御两个等离子体源的影响,即Ar驱动的MHz-Jet KINPen和氦驱动的RF-Jet Cost-Jet。用液-质联用法分析多肽分子结构的变化。氨基酸半胱氨酸、蛋氨酸、酪氨酸和色氨酸被确定为主要目标。最常见的修饰是引入一个、两个或三个氧原子。观察到了不同的硝化(+N + 2O-H)和氯离子(原子氧/次氯酸盐)存在下仅在KINPen中发生的氯化(+Cl-H)和Cost-Jet独有的氯化(+Cl-H)的修饰模式。主要是对于KINPen,观察到了与单线态氧相关的修饰,例如色氨酸的裂解。氧化、羰化和双氧化是由于羟基自由基和原子氧的影响而引起的。这些oxPTM类修饰导致多肽侧链发生显著变化,影响氨基酸链的二级结构和氨基酸的极性/功能,最终改变细胞蛋白质的性能和稳定性。
The effluence of physical plasma consists of a significant share of reactive species, which may interact with biomolecules and yield chemical modifications comparable to those of physiological processes, e.g., post-translational protein modifications (oxPTMs). Consequentially, the aim of this work is to understand the role of physical plasma-derived reactive species in the introduction of oxPTM-like modifications in proteins. An artificial peptide library consisting of ten peptides was screened against the impact of two plasma sources, the argon-driven MHz-jet kINPen and the helium-driven RF-jet COST-Jet. Changes in the peptide molecular structure were analyzed by liquid chromatography–mass spectrometry. The amino acids cysteine, methionine, tyrosine, and tryptophan were identified as major targets. The introduction of one, two, or three oxygen atoms was the most common modification observed. Distinct modification patterns were observed for nitration (+N + 2O–H), which occurred in kINPen only (peroxynitrite), and chlorination (+Cl–H) that was exclusive for the COST-Jet in the presence of chloride ions (atomic oxygen/hypochlorite). Predominantly for the kINPen, singlet oxygen-related modifications, e.g., cleavage of tryptophan, were observed. Oxidation, carbonylation, and double oxidations were attributed to the impact of hydroxyl radicals and atomic oxygen. Leading to a significant change in the peptide side chain, most of these oxPTM-like modifications affect the secondary structure of amino acid chains, and amino acid polarity/functionality, ultimately modifying the performance and stability of cellular proteins.
DOI: 10.1146/annurev.biochem.78.070907.103047
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