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Updated: Oct 1, 2025

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
Published on: April 10, 2020
Selective detection of protein acetylation by NMR spectroscopy
Kyungryun Lee1, Sho Hee Park1, Jung Ho Lee2
1Department of Chemistry, Seoul National University, Seoul 08826, South Korea.
Abstract:
Selective detection of biomolecules and their modifications in cells is essential for understanding cell functions and diseases. We have developed an NMR pulse sequence, Ac-FIND (Acetylation-FIltered aNd eDited), which uses isotope editing/filtering techniques for selective detection of protein acetylation. Acetylation of the N-terminus and lysine side chains by N-succinimidyl acetate was selectively observed for intrinsically disordered α-synuclein and well-ordered ubiquitin. Furthermore, when nonacetylated 13C/15N-enriched α-synuclein was introduced into live HEK293 cells, intracellular N-terminal acetylation of α-synuclein was detected by the appearance of a single peak using Ac-FIND. This work demonstrates the utility of NMR to detect a specific protein modification both in vitro and in live cells.
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