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Fluorogenic probes for detecting deacylase and demethylase activity towards post-translationally-modified lysine residues.

Yuichiro HoriMiyako NishiuraTomomi TaoReisuke BabaSteven D BullKazuya Kikuchi
Published in: Chemical science (2021)
Reversible enzymatic post-translational modification of the ε-amino groups of lysine residues (e.g. N-acylation reactions) plays an important role in regulating the cellular activities of numerous proteins. This study describes how enzyme catalyzed N-deprotection of lysine residues of non-fluorescent peptide-coumarin probes can be used to generate N-deprotected peptides that undergo spontaneous O- to N-ester transfer reactions (uncatalyzed) to generate a highly fluorescent N-carbamoyl peptide. This enables detection of enzyme catalyzed N-deacetylation, N-demalonylation, N-desuccinylation and N-demethylation reactions activities towards the N-modified lysine residues of these probes using simple 'turn on' fluorescent assays.
Keyphrases
  • living cells
  • fluorescent probe
  • single molecule
  • amino acid
  • label free
  • small molecule
  • quantum dots
  • room temperature
  • fluorescence imaging
  • high throughput
  • hydrogen peroxide