Issue 34, 2020

Peptide late-stage C(sp3)–H arylation by native asparagine assistance without exogenous directing groups

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.

Graphical abstract: Peptide late-stage C(sp3)–H arylation by native asparagine assistance without exogenous directing groups

Supplementary files

Article information

Article type
Edge Article
Submitted
13 juil. 2020
Accepted
11 août 2020
First published
12 août 2020
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2020,11, 9290-9295

Peptide late-stage C(sp3)–H arylation by native asparagine assistance without exogenous directing groups

Y. Weng, X. Ding, J. C. A. Oliveira, X. Xu, N. Kaplaneris, M. Zhu, H. Chen, Z. Chen and L. Ackermann, Chem. Sci., 2020, 11, 9290 DOI: 10.1039/D0SC03830J

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