Late-stage peptide modification with salicylaldehyde tag enhances affinity for nuclear factor-kappa B essential modulator
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 proinflammatory
transcription factor NFjB. Fluorescence anisotropy screening led to the identification of SA-tagged peptides with higher affinity than the wild-type sequence.
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