Peptide late-stage C(sp3)–H arylation by native asparagine assistance without exogenous directing groups. Issue 34 (21st August 2020)

• Record Type: Journal Article
• Authors: Weng, Yiyi; Ding, Xingxing; Oliveira, João C. A.; Xu, Xiaobin; Kaplaneris, Nikolaos; Zhu, Meijie; Chen, Hantao; Chen, Zhuo; Ackermann, Lutz
• Is Part Of: Chemical science. Volume 11:Issue 34(2020)
• Page Start: 9290
• Page End: 9295
• Publication Date: 2020-08-21
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/d0sc03830j
• Languages: English
• ISSNs: 2041-6520

Abstract

Abstract : 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. 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(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.