Emerging opportunities for intact and native protein analysis using chemical proteomics

IF 5.7 2区 化学 Q1 CHEMISTRY, ANALYTICAL Analytica Chimica Acta Pub Date : 2024-12-15 DOI:10.1016/j.aca.2024.343551
Alexis N. Edwards, Ku-Lung Hsu
{"title":"Emerging opportunities for intact and native protein analysis using chemical proteomics","authors":"Alexis N. Edwards, Ku-Lung Hsu","doi":"10.1016/j.aca.2024.343551","DOIUrl":null,"url":null,"abstract":"Chemical proteomics has advanced small molecule ligand discovery by providing insights into protein-ligand binding mechanism and enabling medicinal chemistry optimization of protein selectivity on a global scale. Mass spectrometry is the predominant analytical method for chemoproteomics, and various approaches have been deployed to investigate and target a rapidly growing number of protein classes and biological systems. Two methods, intact mass analysis (IMA) and top-down proteomics (TDMS), have gained interest in recent years due to advancements in high resolution mass spectrometry instrumentation. Both methods apply mass spectrometry analysis at the proteoform level, as opposed to the peptide level of bottom-up proteomics (BUMS), thus addressing some of the challenges of protein inference and incomplete information on modification stoichiometry. This Review covers recent research progress utilizing MS-based proteomics methods, discussing in detail the capabilities and opportunities for improvement of each method. Further, heightened attention is given to IMA and TDMS, highlighting these methods’ strengths and considerations when utilized in chemoproteomic studies. Finally, we discuss the capabilities of native mass spectrometry (nMS) and how it can be used in chemoproteomics research to complement existing approaches to further advance the field of functional proteomics.","PeriodicalId":240,"journal":{"name":"Analytica Chimica Acta","volume":"66 1","pages":""},"PeriodicalIF":5.7000,"publicationDate":"2024-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Analytica Chimica Acta","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1016/j.aca.2024.343551","RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, ANALYTICAL","Score":null,"Total":0}
引用次数: 0

Abstract

Chemical proteomics has advanced small molecule ligand discovery by providing insights into protein-ligand binding mechanism and enabling medicinal chemistry optimization of protein selectivity on a global scale. Mass spectrometry is the predominant analytical method for chemoproteomics, and various approaches have been deployed to investigate and target a rapidly growing number of protein classes and biological systems. Two methods, intact mass analysis (IMA) and top-down proteomics (TDMS), have gained interest in recent years due to advancements in high resolution mass spectrometry instrumentation. Both methods apply mass spectrometry analysis at the proteoform level, as opposed to the peptide level of bottom-up proteomics (BUMS), thus addressing some of the challenges of protein inference and incomplete information on modification stoichiometry. This Review covers recent research progress utilizing MS-based proteomics methods, discussing in detail the capabilities and opportunities for improvement of each method. Further, heightened attention is given to IMA and TDMS, highlighting these methods’ strengths and considerations when utilized in chemoproteomic studies. Finally, we discuss the capabilities of native mass spectrometry (nMS) and how it can be used in chemoproteomics research to complement existing approaches to further advance the field of functional proteomics.

Abstract Image

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
利用化学蛋白质组学分析完整蛋白质和原生蛋白质的新机遇
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 去求助
来源期刊
Analytica Chimica Acta
Analytica Chimica Acta 化学-分析化学
CiteScore
10.40
自引率
6.50%
发文量
1081
审稿时长
38 days
期刊介绍: Analytica Chimica Acta has an open access mirror journal Analytica Chimica Acta: X, sharing the same aims and scope, editorial team, submission system and rigorous peer review. Analytica Chimica Acta provides a forum for the rapid publication of original research, and critical, comprehensive reviews dealing with all aspects of fundamental and applied modern analytical chemistry. The journal welcomes the submission of research papers which report studies concerning the development of new and significant analytical methodologies. In determining the suitability of submitted articles for publication, particular scrutiny will be placed on the degree of novelty and impact of the research and the extent to which it adds to the existing body of knowledge in analytical chemistry.
期刊最新文献
Review on activity-based detection of doping substances and growth promotors in biological matrices: do bioassays deserve a place in control programs? Look but don't touch: Non-invasive chemical analysis of organic paint binders - A review. Spatiotemporal metabolic mapping of ex-situ preserved hearts subjected to dialysis by integration of bio-SPME sampling with non-targeted metabolipidomic profiling Corrigendum to “A liquid crystal-decorated aptasensing gadget for rapid monitoring of A549 cells: Future portable test kit for lung cancer diagnosis” [Anal. Chim. Acta. 1330 (2024), 343276-343285] Corrigendum to “A label-free liquid crystal-assisted aptasensor for trace level detection of tobramycin in milk and chicken egg samples” [Anal. Chim. Acta, 1236 (2022), 340588]
×
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
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 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 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1