光催化
化学
亲核细胞
肽
组合化学
表面改性
选择性
催化作用
残留物(化学)
翻译后修饰
有机化学
光催化
生物化学
酶
物理化学
作者
Ping Wang,Qingqing Zhou,Siyao Wang,Xiaheng Zhang
标识
DOI:10.1002/anie.202111388
摘要
Site-selective peptide functionalization provides a straightforward and cost-effective access to diversify peptides for biological studies. Among many existing non-invasive peptide conjugations methodologies, photoredox catalysis has emerged as one of the powerful approaches for site-specific manipulation on native peptides. Herein, we report a highly N-termini-specific method to rapidly access itaconated peptides and their derivatives through a combination of transamination and photoredox conditions. This strategy exploits the facile reactivity of peptidyl-dihydropyridine in the complex peptide settings, complementing existing approaches for bioconjugations with excellent selectivity under mild conditions. Distinct from conventional methods, this method utilizes the highly reactive carbamoyl radical derived from a peptidyl-dihydropyridine. In addition, this itaconated peptide can be further functionalized as a Michael acceptor to access the corresponding peptide-protein conjugate.
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