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

IF 14.4 1区 化学 Q1 CHEMISTRY, MULTIDISCIPLINARY
Qinglong Qiao, Chao Wang, Hanlixin Wang, Yiyan Ruan, Wenjuan Liu, Jie Chen, Zhimin Wu, Xiaogang Liu, Zhaochao Xu
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引用次数: 0

摘要

激发态分子内质子转移(ESIPT)荧光团由于其微环境敏感性而对比例生物成像有价值,但传统的烯醇-酮体系在极性质子环境中存在生物相容性差和效率降低的问题。在这里,我们介绍了一种尾辅助ESIPT (ta-ESIPT)策略,其中质子从酰胺供体转移到氨基氮受体。该机制适用于生物相容性电荷转移荧光团,如萘酰亚胺、香豆素、NBD和乙酰丹。ta-ESIPT荧光团表现出广泛的环境稳定性和水合门控反应─质子转移在水环境中受到抑制,但在非水微环境中恢复,产生比例红移发射。这一特性使生物分子相互作用的精确可视化成为可能。通过将ta-ESIPT荧光团与蛋白质配体偶联,我们实现了活细胞中SNAP-tag、hCA、avidin和HaloTag等靶标的精确比例成像,荧光信号与结合亲和力直接相关。这种相关性能够实时监测蛋白质相互作用和抑制剂的评估,同时最大限度地减少复杂细胞环境中的非特异性干扰,确保动态和准确的蛋白质识别。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Tail-Assisted Excited-State Intramolecular Proton Transfer (ta-ESIPT) Fluorophores: A Universal Ratiometric Platform for Hydration-Sensitive Biomolecular Imaging and Sensing

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.
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来源期刊
CiteScore
24.40
自引率
6.00%
发文量
2398
审稿时长
1.6 months
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.
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