ArticleJournal of mass spectrometry : JMS2012
The reactivity of human serum albumin toward trans-4-hydroxy-2-nonenal.
Article in Journal of mass spectrometry : JMS, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- The unique reactivity of EKODE lipid peroxidation products allows in vivo detection of inflammation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Arginine-Selective Bioconjugation Reagent for EffectiveJournal of medicinal chemistry · 2024Article
- Site-Specific Albumin-Selective Ligation to Human Serum Albumin under Physiological Conditions.Bioconjugate chemistry · 2022Article
- Getting the Right Grip? How Understanding Electrophile Selectivity Profiles Could Illuminate Our Understanding of Redox Signaling.Antioxidants & redox signaling · 2020Article
- Recent trends in protein and peptide-based biomaterials for advanced drug delivery.Advanced drug delivery reviews · 2020Review
- Inhibition effect of pyridoxamine on lipid hydroperoxide-derived modifications to human serum albumin.PloS one · 2018Article
- Site-specific covalent modifications of human insulin by catechol estrogens: Reactivity and induced structural and functional changes.Scientific reports · 2016Article
- 4-Hydroxy-nonenal-A Bioactive Lipid Peroxidation Product.Biomolecules · 2015Review
- Covalent modification of human serum albumin by the natural sesquiterpene lactone parthenolide.Molecules (Basel, Switzerland) · 2015Article
- Quantitative chemoproteomics for site-specific analysis of protein alkylation by 4-hydroxy-2-nonenal in cells.Analytical chemistry · 2015Article
- Site-specific Labeling of a Protein Lysine Residue By Novel Kinetic Labeling Combinatorial Libraries.Computational and structural biotechnology journal · 2014Article
- Carbonylation of mitochondrial aconitase with 4-hydroxy-2-(E)-nonenal: localization and relative reactivity of addition sites.Biochimica et biophysica acta · 2013Article
- Structural mechanism of ring-opening reaction of glucose by human serum albumin.The Journal of biological chemistry · 2013Article
- Comparing the efficiencies of hydrazide labels in the study of protein carbonylation in human serum albumin.Analytical and bioanalytical chemistry · 2012Article
- A Robust Analytical Approach for the Identification of Specific Protein Carbonylation Sites: Metal-Catalyzed Oxidations of Human Serum Albumin.Analytical lettersArticle
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Mass spectrometry was used to probe the preferred locations of trans-4-hydroxy-2-nonenal (HNE) addition to the cysteine, histidine, and lysine residues of human serum albumin (HSA). Considering only those modified peptides supported by high mass accuracy Orbitrap precursor ion measurements (high confidence hits), with HNE:HSA ratios of 1:1 and 10:1, 3 and 15 addition sites, respectively, were identified. Using less stringent criteria, a total of 34 modifications were identified at the higher concentration. To gain quantitative data, iTRAQ labeling studies were completed. Previous work had identified Cys(34) , the only free cysteine, as the most reactive residue in HSA, and we have found that Lys(199) , His(242/7) , and His(288) are the next most reactive residues. Although the kinetic data indicate that the lysines and histidines can react at relatively similar rates, the results show that lysine addition is much less favorable thermodynamically; under our reaction conditions, lysine addition generally does not go to completion. This suggests that under physiological conditions, HNE addition to lysine is only relevant in situations where unusually high HNE concentrations or access to irreversible secondary reactions are found.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.