Mimetics of ADP-ribosylated histidine through copper(I)-catalyzed click chemistry

Author(s):
Minnee, H.; Rack, J.G.M.; Marel, G.A. van der (0000-0001-8917-3458); Overkleeft, H.S. (0000-0001-6992-4760); Codee, J.D.C. (0000-0003-3531-2138); Ahel, I.; Filippov, D.V. (0000-0002-6978-7425)
Published
2022
Publication type
Article / Letter to editor

Abstract

A convergent synthesis provided nearly perfect tau-ADP-ribosylated histidine isosteres (His*-tau-ADPr) via a copper(I)-catalyzed cycloaddition between an azido-ADP-ribosyl analogue and an oligopeptide carrying a propargyl glycine. Both alpha- and beta-configured azido-ADP-ribosyl analogues have been synthesized. The former required participation of the C-2 ester functionality during glycosylation, while the latter was obtained in high stereoselectivity from an imidate donor with a nonparticipating para-methoxy benzyl ether. Four His*-tau-ADPr peptides were screened against a library of human ADP-ribosyl hydrolases.

Date issued
2022-05-19
Language
English
Publisher
AMER CHEMICAL SOC
Is part of
Organic Letters (2022), Vol. 24, no. 21, p. 3776-3780
hdl
1887/3453567
doi
10.1021/acs.orglett.2c01300
URL
https://pubs.acs.org/doi/10.1021/acs.orglett.2c01300