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The molecular ion peak of a molecule in the mass spectrum provides vital information for molecular identification. However, conventional electron impact ionization can lead to the rapid dissociation of some molecular ions before they reach the detector. A milder ionization method is required to increase the lifetime of such ionized analyte molecules. Chemical ionization (CI) is a gas-phase protonation reaction useful for mass-analyzing analyte molecules that are easily protonated to yield the...

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Related Experiment Video

Updated: Jun 29, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

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Published on: April 4, 2018

A Chemical Proteomics Method to Quantify Cysteine S-Acylation.

Chloé Freyermuth¹, Jean-William Dupuy², Thibaud T Renault³

¹Univ. Bordeaux, CNRS, Bordeaux INP, CBMN, UMR 5248, IECB, F-33600 Pessac, France.

ACS Chemical Biology

|January 13, 2026

Summary

This study introduces a new method to precisely quantify protein S-acylation, a crucial modification affecting cell function and disease. The workflow enables large-scale S-acylation analysis, revealing dynamic changes during autophagy.

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Last Updated: Jun 29, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

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Published on: April 4, 2018

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Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

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Published on: June 21, 2021

Area of Science:

Biochemistry
Proteomics
Cellular Biology

Background:

S-acylation (S-palmitoylation) is a reversible posttranslational modification involving fatty acid addition to cysteine residues.
While mass spectrometry has identified many S-acylated proteins, precise quantification of S-acylation levels at the proteome-wide scale remains challenging.
Accurate quantification is vital for understanding S-acylation's role in cellular processes, health, and disease.

Purpose of the Study:

To develop and optimize a robust workflow for the precise, quantitative analysis of S-acylation across the proteome.
To enable the quantification of S-acylation levels for individual cysteine residues within biological samples.
To apply the developed workflow to investigate dynamic S-acylation changes in response to cellular stimuli.

Main Methods:

Developed a quantitative workflow utilizing sequential labeling of free and S-acylated cysteine residues with isotopic reagents.
Optimized the workflow by comparing alkyne-tagged probes and azido-tagged capture reagents for site identification.
Integrated the workflow with high-field asymmetric waveform ion mobility spectrometry (FAIMS) coupled with LC-MS/MS for peptide separation.

Main Results:

Quantified over 17,000 unique cysteine residues in biological samples using the enhanced workflow.
Successfully applied the workflow to quantify S-acylation levels in a HeLa cell proteome.
Identified dynamic alterations in S-acylation in response to autophagy induction.

Conclusions:

The developed S-acylation quantification workflow significantly advances the ability to measure S-acylation levels proteome-wide.
This method provides a powerful tool for dissecting the functional roles of S-acylation in cellular signaling and disease pathogenesis.
The workflow revealed dynamic S-acylation changes associated with autophagy, highlighting its utility in studying dynamic posttranslational modifications.