ArticleAntioxidants (Basel, Switzerland)2018
Unbiased Identification of Proteins Covalently Modified by Complex Mixtures of Peroxidized Lipids Using a Combination of Electrophoretic Mobility Band Shift with Mass Spectrometry.
Article in Antioxidants (Basel, Switzerland), 2018. 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, 13 citations in OpenAlex.
- Peptide-functionalized nanoemulsions with exendin-4 as a model ligand.International journal of pharmaceutics: X · 2026Article
- Major Cat Allergen Fel d 4: Structure and Identification of a Cross-Reactive IgE-Epitope-Containing Area.Allergy · 2026Article
- Effect of TraN key residues involved in DNA binding on pIP501 transfer rates inFrontiers in molecular biosciences · 2024Article
- Pharmacological heat-shock protein inducers and chemical chaperones inhibit upregulation of interleukin-8 by oxidized phospholipids.Inflammopharmacology · 2023Article
- Low Concentrations of Oxidized Phospholipids Increase Stress Tolerance of Endothelial Cells.Antioxidants (Basel, Switzerland) · 2022Article
- Small Things Matter: The 11.6-kDa TraB Protein is Crucial for Antibiotic Resistance Transfer Among Enterococci.Frontiers in molecular biosciences · 2022Article
- Lipid peroxidation derived reactive carbonyl species in free and conjugated forms as an index of lipid peroxidation: limits and perspectives.Redox biology · 2021Article
- Protein Lipoxidation: Basic Concepts and Emerging Roles.Antioxidants (Basel, Switzerland) · 2021Review
- Thiyl Radical Reactions in the Chemical Degradation of Pharmaceutical Proteins.Molecules (Basel, Switzerland) · 2019Review
- Mass Spectrometry-Based Methodologies for Targeted and Untargeted Identification of Protein Covalent Adducts (Adductomics): Current Status and Challenges.High-throughput · 2019Review
- Antioxidants and Second Messengers of Free Radicals.Antioxidants (Basel, Switzerland) · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Covalent modification of functionally important cell proteins by lipid oxidation products (LOPs) is a known mechanism initiating pathological consequences of oxidative stress. Identification of new proteins covalently modified by electrophilic lipids can be performed by a combination of chemical, immunological, and mass spectrometry-based methods, but requires prior knowledge either on the exact molecular structure of LOPs (e.g., 4-hydroxynonenal) or candidate protein targets. However, under the conditions of oxidative stress in vivo, a complex mixture of proteins (e.g., cytosolic proteome) reacts with a complex mixture of LOPs. Here we describe a method for detection of lipid-modified proteins that does not require an a priori knowledge on the chemical structure of LOPs or identity of target proteins. The method is based on the change of electrophoretic mobility of lipid-modified proteins, which is induced by conformational changes and cross-linking with other proteins. Abnormally migrating proteins are detected by mass spectrometry-based protein peptide sequencing. We applied this method to study effects of oxidized palmitoyl-arachidonoyl-phosphatidylcholine (OxPAPC) on endothelial cells. Several known, but also many new, OxPAPC-binding proteins were identified. We expect that this technically relatively simple method can be widely applied for label-free analysis of lipid-protein interactions in complex protein samples treated with different LOPs.
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