期刊
NATURE COMMUNICATIONS
卷 12, 期 1, 页码 -出版社
NATURE PORTFOLIO
DOI: 10.1038/s41467-021-23462-9
关键词
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资金
- DFG (Gottfried-Wilhelm-Leibniz Prize)
- Onassis Foundation
- OPTIMA [EP/L016559/1]
- ERC [307535, 771443]
- DFG (SPP1807)
- European Research Council (ERC) [771443, 307535] Funding Source: European Research Council (ERC)
Bioorthogonal diversification of peptides usually relies on impractical prefunctionalization methods. The authors have developed a manganese(I)-catalyzed C-H fluorescent labeling with BODIPY probes, which enables the development of activatable fluorophores for imaging cell function.
Bioorthogonal late-stage diversification of amino acids and peptides bears enormous potential for drug discovery and molecular imaging. Despite major accomplishments, these strategies largely rely on traditional, lengthy prefunctionalization methods, heavily involving precious transition-metal catalysis. Herein, we report on a resource-economical manganese(I)-catalyzed C-H fluorescent labeling of structurally complex peptides ensured by direct alkynylation and alkenylation manifolds. This modular strategy sets the stage for unraveling structure-activity relationships between structurally discrete fluorophores towards the rational design of BODIPY fluorogenic probes for real-time analysis of immune cell function. Bioorthogonal diversification of peptides is generally dependent on impractical prefunctionalization methods. Here, the authors develop a manganese(I)-catalyzed C-H fluorescent labeling with BODIPY probes, which enables the development of activatable fluorophores to image cell function.
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