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Site-selective aqueous C–H acylation of tyrosine-containing oligopeptides with aldehydes

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Abstract

The development of useful synthetic tools to label amino acids within a peptide framework for the ultimate modification of proteins in a late-stage fashion is a challenging task of utmost importance within chemical biology. Herein, we report the first Pd-catalyzed C–H acylation of a collection of Tyr-containing peptides with aldehydes. This water-compatible tagging technique is distinguished by its site-specificity, scalability and full tolerance of sensitive functional groups. Remarkably, it provides straightforward access to a high number of oligopeptides with altered side-chain topology including mimetics of endomorphin-2 and neuromedin N, thus illustrating its promising perspectives toward the diversification of structurally complex peptides and chemical ligation.

Graphical abstract: Site-selective aqueous C–H acylation of tyrosine-containing oligopeptides with aldehydes

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Article information


Submitted
11 Jul 2020
Accepted
30 Sep 2020
First published
06 Oct 2020

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2020, Advance Article
Article type
Edge Article

Site-selective aqueous C–H acylation of tyrosine-containing oligopeptides with aldehydes

M. San Segundo and A. Correa, Chem. Sci., 2020, Advance Article , DOI: 10.1039/D0SC03791E

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