Rational Tuning of Fluorobenzene Probes for Cysteine-Selective Protein Modification
Rational Tuning of Fluorobenzene Probes for Cysteine-Selective Protein Modification
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DOI：
10.1002/anie.201712589
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发表时间：
2018-07-02
影响因子：
16.6
通讯作者：
Diness, Frederik
中科院分区：
文献类型：
--
作者：
Embaby, Ahmed M.;Schoffelen, Sanne;Diness, Frederik
通过合理的反应性调节，已经开发出用于通过选择性半胱氨酸标记进行蛋白质谱分析的氟苯探针。通过选择吸电子的对位取代基并结合改变氟取代基的数目来实现调节。优化的探针在水条件下化学选择性地使蛋白质中的半胱氨酸残基芳基化。与叠氮、生物素或荧光团相连的探针适用于EGFP和白蛋白的标记。该探针对半胱氨酸蛋白酶也有选择性抑制作用。此外，还调整了探针，用于半胱氨酸残基的选择性标记和细胞裂解产物中基于活性的蛋白质图谱。
Fluorobenzene probes for protein profiling through selective cysteine labeling have been developed by rational reactivity tuning. Tuning was achieved by selecting an electron-withdrawing para substituent in combination with variation of the number of fluorine substituents. Optimized probes chemoselectively arylated cysteine residues in proteins under aqueous conditions. Probes linked to azide, biotin, or a fluorophore were applicable to labeling of eGFP and albumin. Selective inhibition of cysteine proteases was also demonstrated with the probes. Additionally, probes were tuned for site-selective labeling of cysteine residues and for activity-based protein profiling in cell lysates.