Peptide late-stage C(sp3)–H arylation by native asparagine assistance without exogenous directing groups |
| |
| Authors: | Yiyi Weng,Xingxing Ding,Joã o C. A. Oliveira,Xiaobin Xu,Nikolaos Kaplaneris,Meijie Zhu,Hantao Chen,Zhuo Chen,Lutz Ackermann |
| |
| Affiliation: | College of Pharmaceutical Sciences, Zhejiang University of Technology, Hangzhou 310014 P. R. China.; Institut fuer Organische und Biomolekulare Chemie, Georg-August-Universitaet Goettingen, Tammannstrasse 2, Goettingen 37077 Germany, |
| |
| Abstract: | 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(sp3)–H arylations assisted by the unmodified side chain of asparagine (Asn) without any exogenous directing group. Thereby, site-selective arylations of C(sp3)–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(sp3)-H arylations assisted by unmodified side chain of asparagine (Asn) without any exogenous directing group has been reported. |
| |
| Keywords: | |
|
|
