用碰撞诱导的展开来描述PFAS对蛋白质结构的结合效应
Ebunoluwa O Kukoyi1, Kenneth W Lee1
1Brigham Young University, Provo, Utah 84602-1030, United States.
Chemical research in toxicology
|August 15, 2025
概括
和多醇基物质 (PFAS) 可以改变蛋白质结构,可能导致毒性. 循环离子流动性质谱学显示,PFAS结合会根据PFAS链长度和数量不同地影响蛋白质展开.
科学领域:
- 环境化学环境化学
- 生物化学 生物化学
- 毒理学 毒理学 毒理学
背景情况:
- 和多醇基物质 (PFAS) 是持久性环境污染物,由于生物积累,可能会对健康产生不利影响.
- 了解PFAS与蛋白质等生物分子的相互作用,对于阐明它们的毒性机制至关重要.
- 对蛋白质的非共价复合是PFAS诱导的细胞毒性的潜在途径.
研究的目的:
- 通过碰撞诱导展开 (CIU) 研究PFAS结合对蛋白质结构的影响.
- 为了比较不同的PFAS分子在模型蛋白质上具有不同的链长的结构效应.
主要方法:
- 利用循环离子移动性质谱法 (cIM-MS) 进行碰撞诱导展开 (CIU).
- 测量蛋白质大小和形状的变化作为激活能的函数,以描述展开的路径.
- 采用乌比奎丁作为模型蛋白质,并测试了三个相关的PFAS:PFBS,PFHxS和PFOS.
主要成果:
- 观察到的泛素展开的定性和定量差异受到结合的PFAS分子数量的影响.
- 证明PFAS链长度显著影响蛋白质结构变化.
- 展示了PFAS与蛋白质相关联时的非被动作用.
结论:
- CIU-cIM-MS提供了一种快速有针对性的方法,用于分析毒素和生物分子之间的非共价复合.
- 结合PFAS可以诱导蛋白质的独特结构变化,因PFAS的特性而有所不同.
- 这种方法有助于在分子水平上了解潜在的PFAS毒性机制.
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