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

ABSTRACT: 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.

SUBMITTER: Minnee H

PROVIDER: S-EPMC9171823 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature

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

Minnee Hugo H Rack Johannes G M JGM van der Marel Gijsbert A GA Overkleeft Herman S HS Codée Jeroen D C JDC Ahel Ivan I Filippov Dmitri V DV

Organic letters 20220519 21

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 <i>para< ...[more]

PMID: 35587229

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