Late-stage peptide modification with salicylaldehyde tag enhances affinity for nuclear factor-kappa B essential modulator

Abstract

The late-stage peptide functionalization with salicylaldehyde (SA) tags is described here as a versatile design of potential Lys-engaging, reversible-covalent ligands. This approach was applied to a known binder for NEMO, a protein involved in the activation of the pro-inflammatory transcription factor NFκB. Fluorescence anisotropy screening led to the identification of SA-tagged peptides with higher affinity than the wild-type sequence.