{"title":"质谱法反映了铜淀粉样蛋白 β 化学的关键方面。","authors":"Sarah Brandner, Tanja Habeck and Frederik Lermyte","doi":"10.1039/D4AN00693C","DOIUrl":null,"url":null,"abstract":"<p >Mass spectrometry is a powerful method to study protein complexes; however, biochemical reactions are typically beyond the scope of MS studies. Here, we have studied the gas-phase redox chemistry of the [copper(<small>II</small>) – amyloid β] complex and show that the sequence-dependence of this chemistry reflects key aspects of the known <em>in vitro</em> behaviour of different variants of the peptide.</p>","PeriodicalId":63,"journal":{"name":"Analyst","volume":" 24","pages":" 5762-5767"},"PeriodicalIF":3.6000,"publicationDate":"2024-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Mass spectrometry reflects key aspects of copper-amyloid β chemistry†\",\"authors\":\"Sarah Brandner, Tanja Habeck and Frederik Lermyte\",\"doi\":\"10.1039/D4AN00693C\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p >Mass spectrometry is a powerful method to study protein complexes; however, biochemical reactions are typically beyond the scope of MS studies. Here, we have studied the gas-phase redox chemistry of the [copper(<small>II</small>) – amyloid β] complex and show that the sequence-dependence of this chemistry reflects key aspects of the known <em>in vitro</em> behaviour of different variants of the peptide.</p>\",\"PeriodicalId\":63,\"journal\":{\"name\":\"Analyst\",\"volume\":\" 24\",\"pages\":\" 5762-5767\"},\"PeriodicalIF\":3.6000,\"publicationDate\":\"2024-10-07\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Analyst\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://pubs.rsc.org/en/content/articlelanding/2024/an/d4an00693c\",\"RegionNum\":3,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"CHEMISTRY, ANALYTICAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Analyst","FirstCategoryId":"92","ListUrlMain":"https://pubs.rsc.org/en/content/articlelanding/2024/an/d4an00693c","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"CHEMISTRY, ANALYTICAL","Score":null,"Total":0}
Mass spectrometry reflects key aspects of copper-amyloid β chemistry†
Mass spectrometry is a powerful method to study protein complexes; however, biochemical reactions are typically beyond the scope of MS studies. Here, we have studied the gas-phase redox chemistry of the [copper(II) – amyloid β] complex and show that the sequence-dependence of this chemistry reflects key aspects of the known in vitro behaviour of different variants of the peptide.