The Effect of Hypochlorite-Induced Fibrinogen Oxidation on the Protein Structure, Fibrin Self-Assembly, and Fibrinolysis

IF 1.4 4区 化学 Q4 PHYSICS, ATOMIC, MOLECULAR & CHEMICAL
L. V. Yurina, A. D. Vasilyeva, E. G. Evtushenko, E. S. Gavrilina, S. I. Obydennyi, I. A. Chabin, M. I. Indeykina, A. S. Kononikhin, E. N. Nikolaev, M. A. Rosenfeld
{"title":"The Effect of Hypochlorite-Induced Fibrinogen Oxidation on the Protein Structure, Fibrin Self-Assembly, and Fibrinolysis","authors":"L. V. Yurina, A. D. Vasilyeva, E. G. Evtushenko, E. S. Gavrilina, S. I. Obydennyi, I. A. Chabin, M. I. Indeykina, A. S. Kononikhin, E. N. Nikolaev, M. A. Rosenfeld","doi":"10.1134/s1990793124020349","DOIUrl":null,"url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>This article studies the structural-functional damage of fibrinogen (FG) treated with hypochlorous acid (HOCl) in the concentration range (10–100 µM). Using tandem mass spectronomy (the MS/MS method), 15 modified amino acid residues with a dose-dependent susceptibility to the oxidizing agent are detected. Using turbidity measurements and confocal laser scanning microscopy (CLSM), it is shown that FG oxidation by 25–100 µM HOCl leads to the formation of a denser fibrin gel, a delayed onset of polymerization, and a decrease in the slope of the polymerization curve, presumably due to the conformational changes in the protein. At lower a HOCl concentration (10 µM), at least six amino acid residues are substantially modified (9–29%), but functionally such modified protein was not distinguishable from the native one. The detected amino acid residues are assumed to be scavengers of the reactive oxygen species (ROS), which prevent the alteration of FG functions.</p>","PeriodicalId":768,"journal":{"name":"Russian Journal of Physical Chemistry B","volume":null,"pages":null},"PeriodicalIF":1.4000,"publicationDate":"2024-05-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Russian Journal of Physical Chemistry B","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1134/s1990793124020349","RegionNum":4,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"PHYSICS, ATOMIC, MOLECULAR & CHEMICAL","Score":null,"Total":0}
引用次数: 0

Abstract

This article studies the structural-functional damage of fibrinogen (FG) treated with hypochlorous acid (HOCl) in the concentration range (10–100 µM). Using tandem mass spectronomy (the MS/MS method), 15 modified amino acid residues with a dose-dependent susceptibility to the oxidizing agent are detected. Using turbidity measurements and confocal laser scanning microscopy (CLSM), it is shown that FG oxidation by 25–100 µM HOCl leads to the formation of a denser fibrin gel, a delayed onset of polymerization, and a decrease in the slope of the polymerization curve, presumably due to the conformational changes in the protein. At lower a HOCl concentration (10 µM), at least six amino acid residues are substantially modified (9–29%), but functionally such modified protein was not distinguishable from the native one. The detected amino acid residues are assumed to be scavengers of the reactive oxygen species (ROS), which prevent the alteration of FG functions.

Abstract Image

次氯酸盐诱导的纤维蛋白原氧化对蛋白质结构、纤维蛋白自组装和纤维蛋白溶解的影响
摘要 本文研究了纤维蛋白原(FG)在次氯酸(HOCl)浓度(10-100 µM)范围内的结构-功能损伤。利用串联质谱分析法(MS/MS 法),检测了 15 个对氧化剂的敏感性随剂量变化的修饰氨基酸残基。通过浊度测量和共聚焦激光扫描显微镜(CLSM),研究表明 FG 被 25-100 µM HOCl 氧化后会形成更致密的纤维蛋白凝胶,聚合开始时间延迟,聚合曲线斜率降低,这可能是由于蛋白质构象发生了变化。在较低的 HOCl 浓度(10 µM)下,至少有六个氨基酸残基发生了实质性改变(9-29%),但从功能上看,这种改变后的蛋白质与原生蛋白质没有区别。检测到的氨基酸残基被认为是活性氧(ROS)的清除剂,可防止 FG 功能的改变。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Russian Journal of Physical Chemistry B
Russian Journal of Physical Chemistry B 化学-物理:原子、分子和化学物理
CiteScore
2.20
自引率
71.40%
发文量
106
审稿时长
4-8 weeks
期刊介绍: Russian Journal of Physical Chemistry B: Focus on Physics is a journal that publishes studies in the following areas: elementary physical and chemical processes; structure of chemical compounds, reactivity, effect of external field and environment on chemical transformations; molecular dynamics and molecular organization; dynamics and kinetics of photoand radiation-induced processes; mechanism of chemical reactions in gas and condensed phases and at interfaces; chain and thermal processes of ignition, combustion and detonation in gases, two-phase and condensed systems; shock waves; new physical methods of examining chemical reactions; and biological processes in chemical physics.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信