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Updated: Sep 3, 2026
Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021
Quantification of Site-Specific Disulfide Bond Redox States in Proteins by Parallel Reaction Monitoring-Mass
Aizhen Yang1, Yi Wu2, Fengwu Chen3,4
1Cyrus Tang Hematology Center, Cyrus Tang Medical Institute, Soochow University, Suzhou, China. yangaizhen@suda.edu.cn.
Abstract:
Conventional non-targeted approaches using data-dependent acquisition (DDA) with isotopic labeling mass spectrometry (MS) have demonstrated limited effectiveness in characterizing site-specific disulfide bond redox states, primarily due to suboptimal coverage and inconsistent reproducibility. Here, we introduce a targeted approach employing differential cysteine alkylation coupled with parallel reaction monitoring (PRM)-MS to identify the redox states of specific disulfide bond sites in proteins, which significantly improves the coverage and reproducibility of mass spectrometry data.
