ArticleInternational journal of molecular sciences2022
Spontaneous and Ionizing Radiation-Induced Aggregation of Human Serum Albumin: Dityrosine as a Fluorescent Probe.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Peroxynitrite-induced structural remodeling and aggregation of hemoglobin under nitroxidative stress.Protein science : a publication of the Protein Society · 2026Article
- In Vitro Studies of the Effects of Antithrombotic Zn-Dipicolylamine-Harboring Liposomes (DPALs) on Serum Albumin and Human Umbilical Vein Endothelial Cells.International journal of molecular sciences · 2026Article
- Spectroscopic and Pulse Radiolysis Studies of Water-Ethanolic Solutions of Albumins: Insight into Serum Albumin Aggregation.International journal of molecular sciences · 2025Article
- The Molecular Recognition of Lurasidone by Human Serum Albumin: A Combined Experimental and Computational Approach.Molecules (Basel, Switzerland) · 2025Article
- Interaction between albumin originating from persons with uncontrolled diabetes mellitus type 2 and food antioxidants.ADMET & DMPK · 2025Article
- Aggregation of Albumins under Reductive Radical Stress.International journal of molecular sciences · 2024Article
- Self-Assembly of a Novel Pentapeptide into Hydrogelated Dendritic Architecture: Synthesis, Properties, Molecular Docking and Prospective Applications.Gels (Basel, Switzerland) · 2024Article
- Influence of Ionizing Radiation on Spontaneously Formed Aggregates in Proteins or Enzymes Solutions.Pharmaceutics · 2023Article
- Binding of Epimedium Flavonoids to Human Serum Albumin: Insights from Spectroscopic and Molecular Docking Studies.Iranian journal of pharmaceutical research : IJPRArticle
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The use of spectroscopic techniques has shown that human serum albumin (HSA) undergoes reversible self-aggregation through protein−protein interactions. It ensures the subsequent overlapping of electron clouds along with the stiffening of the conformation of the interpenetrating network of amino acids of adjacent HSA molecules. The HSA oxidation process related to the transfer of one electron was investigated by pulse radiolysis and photochemical methods. It has been shown that the irradiation of HSA solutions under oxidative stress conditions results in the formation of stable protein aggregates. The HSA aggregates induced by ionizing radiation are characterized by specific fluorescence compared to the emission of non-irradiated solutions. We assume that HSA dimers are mainly responsible for the new emission. Dityrosine produced by the intermolecular recombination of protein tyrosine radicals as a result of radiolysis of an aqueous solution of the protein is the main cause of HSA aggregation by cross-linking. Analysis of the oxidation process of HSA confirmed that the reaction of mild oxidants (Br2•−, N3•, SO4•−) with albumin leads to the formation of covalent bonds between tyrosine residues. In the case of •OH radicals and partly, Cl2•−, species other than DT are formed. The light emission of this species is similar to the emission of self-associated HSA.
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