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Selective modification of sulfamidate-containing peptides

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Abstract

Hybrid peptides whose N-terminal residues are activated in the form of α-methylisoserine-derived cyclic sulfamidates exhibit rich reactivity as electrophiles, allowing site- and stereoselective modifications at different backbone and side chain positions. The unique properties of this scaffold allow the stereocontrolled late-stage functionalization of the peptide backbone by nucleophilic ring opening with fluorescent probes, thiocarbohydrates and tags for strain-promoted azide–alkyne cycloaddition as well as by installing labile N-terminal affinity tags (biotin) and cytotoxic drugs (chlorambucil) for pH-controlled release. Finally, an unexpected base-promoted acyl group migration from the sulfamidate N-terminus allows fast and quantitative intramolecular modification of nucleophilic side chains on the fully unprotected peptides.

Graphical abstract: Selective modification of sulfamidate-containing peptides

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Supplementary files

Article information


Submitted
22 May 2020
Accepted
23 Jun 2020
First published
23 Jun 2020

Org. Biomol. Chem., 2020, Advance Article
Article type
Paper

Selective modification of sulfamidate-containing peptides

N. Mazo, C. D. Navo, J. M. Peregrina, J. H. Busto and G. Jiménez-Osés, Org. Biomol. Chem., 2020, Advance Article , DOI: 10.1039/D0OB01061H

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