• 主题
高级搜索  >
历史搜索 清空历史
首页> 美国卫生研究院文献>International Journal of Molecular Sciences >Free Radicals and ROS Induce Protein Denaturation by UV Photostability Assay
【2h】

Free Radicals and ROS Induce Protein Denaturation by UV Photostability Assay

机译：通过UV光稳定性测定自由基和ROS诱导蛋白质变性

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务，本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文，但由于OA文献来源多样且变更频繁，仍可能出现获取不到、文献不完整或与标题不符等情况，如果获取不到我们将提供退款服务。请知悉。
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Oxidative stress, photo-oxidation, and photosensitizers are activated by UV irradiation and are affecting the photo-stability of proteins. Understanding the mechanisms that govern protein photo-stability is essential for its control enabling enhancement or reduction. Currently, two major mechanisms for protein denaturation induced by UV irradiation are available: one generated by the local heating of water molecules bound to the proteins and the other by the formation of reactive free radicals. To discriminate which is the likely or dominant mechanism we have studied the effects of thermal and UV denaturation of aqueous protein solutions with and without DHR-123 as fluorogenic probe using circular dichroism (CD), synchrotron radiation circular dichroism (SRCD), and fluorescence spectroscopies. The results indicated that the mechanism of protein denaturation induced by VUV and far-UV irradiation were mediated by the formation of reactive free radicals (FR) and reactive oxygen species (ROS). The development at Diamond B23 beamline for SRCD of a novel protein UV photo-stability assay based on consecutive repeated CD measurements in the far-UV (180–250 nm) region has been successfully used to assess and characterize the photo-stability of protein formulations and ligand binding interactions, in particular for ligand molecules devoid of significant UV absorption.
机译：通过UV辐射激活氧化应激，光氧化和光敏剂，并影响蛋白质的光稳定性。了解控制蛋白质光稳定性的机制对于其控制能够增强或减少至关重要。目前，通过UV照射诱导的蛋白质变性的两个主要机制可获得：通过形成反应自由基的局部水分子的局部加热产生的蛋白质变性的主要机制。为了区分这是我们研究了使用圆形二色（CD），同步辐射圆形二色（SRCD）和荧光光谱法作为荧光探针作为荧光探针的热和UV变性的可能或优势机制。 。结果表明，通过形成活性自由基（FR）和反应性氧（ROS）的形成介导所述VUV和FAR-UV辐射诱导的蛋白质变性机制。基于FAR-UV（180-250nm）区域的连续反复CD测量的新型蛋白质UV光稳定性测定的SRCD的Diamond B23 BeAdlin的开发已成功地用于评估和表征蛋白质配方的光稳定性和配体结合相互作用，特别是对于具有显着紫外线吸收的配体分子。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号