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Weng, Yiyi; Ding, Xingxing; Oliveira, João C. A; Xu, Xiaobin; Kaplaneris, Nikolaos; Zhu, Meijie; Chen, Hantao; Chen, Zhuo; Ackermann, Lutz
Chemical science, 08/2020, Volume: 11, Issue: 34Journal Article
There is a strong demand for novel native peptide motifs for post-synthetic modifications of peptides without pre-installation and subsequent removal of directing groups. Herein, we report an efficient method for peptide late-stage C(sp 3 )-H arylations assisted by the unmodified side chain of asparagine (Asn) without any exogenous directing group. Thereby, site-selective arylations of C(sp 3 )-H bonds at the N-terminus of di-, tri-, and tetrapeptides have been achieved. Likewise, we have constructed a key building block for accessing agouti-related protein (AGRP) active loop analogues in a concise manner. An efficient method for peptide late-stage C(sp 3 )-H arylations assisted by unmodified side chain of asparagine (Asn) without any exogenous directing group has been reported.
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