Abstract：
Peptide modification by C(sp3)-H functionalization of residues at the internal positions remains underdeveloped due to the inhibitory effect of backbone amides. In this study, using histidine (His) as an endogenous directing group, we developed a novel method for the β-C(sp3)-H functionalization of alanine (Ala) at diverse positions of peptides. Through this approach, a wide range of linear peptides were modified on the side-chain of Ala adjacent to His to afford the functionalized peptides in moderate to good yield and excellent position selectivity. Furthermore, conjugation of peptides with functional molecules such as glucuronide, oleanolic acid, dipeptide, and fluorophore derivatives was achieved.
摘要：
由于主链酰胺的抑制作用,通过内部位置处的残基的C(sp3)-H官能化的肽修饰仍然不发达。在这项研究中,使用组氨酸（His）作为内源性指导基团，我们开发了一种在肽的不同位置对丙氨酸（Ala）进行β-C（sp3）-H官能化的新方法。通过这种方法，在邻近His的Ala的侧链上修饰宽范围的线性肽,从而以中等至良好的产率和优异的位置选择性提供官能化的肽。此外，肽与功能分子如葡糖苷酸的缀合，齐墩果酸，二肽，并获得荧光团衍生物。
