Mimetics of ADP-Ribosylated Histidine through Copper(I)-Catalyzed Click Chemistry

A convergent synthesis provided nearly perfect τ-ADP-ribosylated histidine isosteres (His*-τ-ADPr) via a copper­(I)-catalyzed cycloaddition between an azido-ADP-ribosyl analogue and an oligopeptide carrying a propargyl glycine. Both α- and β-configured azido-ADP-ribosyl analogues have been synthesiz...

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Bibliographic Details
Published in:Organic letters 2022-06, Vol.24 (21), p.3776-3780
Main Authors: Minnee, Hugo, Rack, Johannes G. M., van der Marel, Gijsbert A., Overkleeft, Herman S., Codée, Jeroen D. C., Ahel, Ivan, Filippov, Dmitri V.
Format: Article
Language:English
Subjects:
Adenosine Diphosphate
Catalysis
Click Chemistry
Copper
Histidine
Humans
Letter
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Summary:A convergent synthesis provided nearly perfect τ-ADP-ribosylated histidine isosteres (His*-τ-ADPr) via a copper­(I)-catalyzed cycloaddition between an azido-ADP-ribosyl analogue and an oligopeptide carrying a propargyl glycine. Both α- and β-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*-τ-ADPr peptides were screened against a library of human ADP-ribosyl hydrolases.
ISSN:1523-7060
1523-7052
DOI:10.1021/acs.orglett.2c01300