Institut für Organische und Biomolekulare Chemie, Georg-August-Universität Göttingen, Göttingen, Germany.
Centre for Inflammation Research, The University of Edinburgh, Edinburgh, UK.
Nat Commun. 2021 Jun 7;12(1):3389. doi: 10.1038/s41467-021-23462-9.
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.
生物正交的氨基酸和肽的后期多样化在药物发现和分子成像方面具有巨大的潜力。尽管取得了重大成就，但这些策略在很大程度上依赖于传统的、冗长的预功能化方法，大量涉及宝贵的过渡金属催化。在此，我们报告了一种通过直接炔基化和烯基化途径实现的结构复杂肽的资源经济的锰（I）催化 C-H 荧光标记。这种模块化策略为揭示结构离散荧光团之间的结构-活性关系奠定了基础，从而为实时分析免疫细胞功能的 BODIPY 荧光探针的合理设计提供了依据。
