Fig. 1: Stapling of unprotected peptides via non-Cys residues under mild aqueous conditions. | Nature Communications

Fig. 1: Stapling of unprotected peptides via non-Cys residues under mild aqueous conditions.

From: Extendable stapling of unprotected peptides by crosslinking two amines with o-phthalaldehyde

Fig. 1

a Common strategies for peptide stapling via two cysteine residues. b OPA-mediated peptide stapling via cysteine and lysine residues. c OPA-mediated peptide stapling via two amine groups (this work). C: cysteine, K: lysine. The thiol group of cysteine is marked in magenta. The amino group is marked in red. The linkers joining the two cysteines are marked in cayenne. The OPA reagent and isoindolinimine core are marked in green. The π electrophiles are marked in mocha. The linkages between isoindolinimine and electrophiles are marked in blue.

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