{"title":"尾部辅助激发态分子内质子转移(ta-ESIPT)荧光团:水合敏感生物分子成像和传感的通用比率测量平台","authors":"Qinglong Qiao, Chao Wang, Hanlixin Wang, Yiyan Ruan, Wenjuan Liu, Jie Chen, Zhimin Wu, Xiaogang Liu, Zhaochao Xu","doi":"10.1021/jacs.5c02725","DOIUrl":null,"url":null,"abstract":"Excited-state intramolecular proton transfer (ESIPT) fluorophores are valuable for ratiometric bioimaging due to their microenvironmental sensitivity, but traditional enol–keto systems suffer from poor biocompatibility and reduced efficiency in polar, protic environments. Here, we introduce a tail-assisted ESIPT (<i>ta</i>-ESIPT) strategy in which proton transfer occurs from an amide donor to an amino nitrogen acceptor. This mechanism applies to biocompatible charge-transfer fluorophores, such as naphthalimide, coumarin, NBD, and acedan. <i>ta</i>-ESIPT fluorophores exhibit broad environmental stability and a hydration-gated response─proton transfer is inhibited in aqueous environments but restored in nonaqueous microenvironments, yielding ratiometric red-shifted emission. This property enables the precise visualization of biomolecular interactions. By conjugating <i>ta</i>-ESIPT fluorophores with protein ligands, we achieve precise, ratiometric imaging of targets like SNAP-tag, hCA, avidin, and HaloTag in live cells, with fluorescence signals that directly correlate with binding affinities. This correlation enables real-time monitoring of protein interactions and evaluation of inhibitors while minimizing nonspecific interference in the complex cellular environment, ensuring dynamic and accurate protein recognition.","PeriodicalId":49,"journal":{"name":"Journal of the American Chemical Society","volume":"37 1","pages":""},"PeriodicalIF":14.4000,"publicationDate":"2025-04-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Tail-Assisted Excited-State Intramolecular Proton Transfer (ta-ESIPT) Fluorophores: A Universal Ratiometric Platform for Hydration-Sensitive Biomolecular Imaging and Sensing\",\"authors\":\"Qinglong Qiao, Chao Wang, Hanlixin Wang, Yiyan Ruan, Wenjuan Liu, Jie Chen, Zhimin Wu, Xiaogang Liu, Zhaochao Xu\",\"doi\":\"10.1021/jacs.5c02725\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Excited-state intramolecular proton transfer (ESIPT) fluorophores are valuable for ratiometric bioimaging due to their microenvironmental sensitivity, but traditional enol–keto systems suffer from poor biocompatibility and reduced efficiency in polar, protic environments. Here, we introduce a tail-assisted ESIPT (<i>ta</i>-ESIPT) strategy in which proton transfer occurs from an amide donor to an amino nitrogen acceptor. This mechanism applies to biocompatible charge-transfer fluorophores, such as naphthalimide, coumarin, NBD, and acedan. <i>ta</i>-ESIPT fluorophores exhibit broad environmental stability and a hydration-gated response─proton transfer is inhibited in aqueous environments but restored in nonaqueous microenvironments, yielding ratiometric red-shifted emission. This property enables the precise visualization of biomolecular interactions. By conjugating <i>ta</i>-ESIPT fluorophores with protein ligands, we achieve precise, ratiometric imaging of targets like SNAP-tag, hCA, avidin, and HaloTag in live cells, with fluorescence signals that directly correlate with binding affinities. This correlation enables real-time monitoring of protein interactions and evaluation of inhibitors while minimizing nonspecific interference in the complex cellular environment, ensuring dynamic and accurate protein recognition.\",\"PeriodicalId\":49,\"journal\":{\"name\":\"Journal of the American Chemical Society\",\"volume\":\"37 1\",\"pages\":\"\"},\"PeriodicalIF\":14.4000,\"publicationDate\":\"2025-04-25\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of the American Chemical Society\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://doi.org/10.1021/jacs.5c02725\",\"RegionNum\":1,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of the American Chemical Society","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1021/jacs.5c02725","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
Tail-Assisted Excited-State Intramolecular Proton Transfer (ta-ESIPT) Fluorophores: A Universal Ratiometric Platform for Hydration-Sensitive Biomolecular Imaging and Sensing
Excited-state intramolecular proton transfer (ESIPT) fluorophores are valuable for ratiometric bioimaging due to their microenvironmental sensitivity, but traditional enol–keto systems suffer from poor biocompatibility and reduced efficiency in polar, protic environments. Here, we introduce a tail-assisted ESIPT (ta-ESIPT) strategy in which proton transfer occurs from an amide donor to an amino nitrogen acceptor. This mechanism applies to biocompatible charge-transfer fluorophores, such as naphthalimide, coumarin, NBD, and acedan. ta-ESIPT fluorophores exhibit broad environmental stability and a hydration-gated response─proton transfer is inhibited in aqueous environments but restored in nonaqueous microenvironments, yielding ratiometric red-shifted emission. This property enables the precise visualization of biomolecular interactions. By conjugating ta-ESIPT fluorophores with protein ligands, we achieve precise, ratiometric imaging of targets like SNAP-tag, hCA, avidin, and HaloTag in live cells, with fluorescence signals that directly correlate with binding affinities. This correlation enables real-time monitoring of protein interactions and evaluation of inhibitors while minimizing nonspecific interference in the complex cellular environment, ensuring dynamic and accurate protein recognition.
期刊介绍:
The flagship journal of the American Chemical Society, known as the Journal of the American Chemical Society (JACS), has been a prestigious publication since its establishment in 1879. It holds a preeminent position in the field of chemistry and related interdisciplinary sciences. JACS is committed to disseminating cutting-edge research papers, covering a wide range of topics, and encompasses approximately 19,000 pages of Articles, Communications, and Perspectives annually. With a weekly publication frequency, JACS plays a vital role in advancing the field of chemistry by providing essential research.