ArticleAntioxidants (Basel, Switzerland)2021
A Workflow towards the Reproducible Identification and Quantitation of Protein Carbonylation Sites in Human Plasma.
Article in Antioxidants (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Screening of Protein Carbonylation Sites in Human Serum by Ion Mobility Mass Spectrometry.Journal of proteome research · 2025Article
- Molecular, Physical, and Technical Performance Response After a Competitive Match in Male Professional Soccer Players.Antioxidants (Basel, Switzerland) · 2025Article
- Immunoproteomics enable broad identification of newFrontiers in immunology · 2024Article
- Article
- Iron Availability Influences Protein Carbonylation inInternational journal of molecular sciences · 2023Article
- Article
- Immunoproteomics reveal increased serum IgG3/5 binding toFrontiers in immunology · 2023Article
- Evaluation of Sample Preparation Strategies for Human Milk and Plasma Proteomics.Molecules (Basel, Switzerland) · 2021Article
- Analysis of the Endogenous Peptidomes of Different Infant Formula Types and Human Milk.Foods (Basel, Switzerland) · 2021Article
- Reactive Carbonyl Species and Protein Adducts: Identification Strategies, Biological Mechanisms and Molecular Approaches for Their Detoxification.Antioxidants (Basel, Switzerland) · 2021Article
- Identification of Disease-Associated Cryptococcal Proteins Reactive With Serum IgG From Cryptococcal Meningitis Patients.Frontiers in immunology · 2021Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Protein carbonylation, a marker of excessive oxidative stress, has been studied in the context of multiple human diseases related to oxidative stress. The variety of post-translational carbonyl modifications (carbonyl PTMs) and their low concentrations in plasma challenge their reproducible identification and quantitation. However, carbonyl-specific biotinylated derivatization tags (e.g., aldehyde reactive probe, ARP) allow for targeting carbonyl PTMs by enriching proteins and peptides carrying these modifications. In this study, an oxidized human serum albumin protein model (OxHSA) and plasma from a healthy donor were derivatized with ARP, digested with trypsin, and enriched using biotin-avidin affinity chromatography prior to nano reversed-phase chromatography coupled online to electrospray ionization tandem mass spectrometry with travelling wave ion mobility spectrometry (nRPC-ESI-MS/MS-TWIMS). The presented workflow addresses several analytical challenges by using ARP-specific fragment ions to reliably identify ARP peptides. Furthermore, the reproducible recovery and relative quantitation of ARP peptides were validated. Human serum albumin (HSA) in plasma was heavily modified by a variety of direct amino acid oxidation products and adducts from reactive carbonyl species (RCS), with most RCS modifications being detected in six hotspots, i.e., Lys10, Lys190, Lys199, Lys281, Lys432, and Lys525 of mature HSA.
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Registered trials
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