{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,14]],"date-time":"2026-09-14T23:23:36Z","timestamp":1789428216336,"version":"build-2803163510"},"reference-count":76,"publisher":"MDPI AG","issue":"15","license":[{"start":{"date-parts":[[2022,7,22]],"date-time":"2022-07-22T00:00:00Z","timestamp":1658448000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004281","name":"National Science Centre","doi-asserted-by":"publisher","award":["2019\/33\/B\/ST5\/02125"],"award-info":[{"award-number":["2019\/33\/B\/ST5\/02125"]}],"id":[{"id":"10.13039\/501100004281","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The use of spectroscopic techniques has shown that human serum albumin (HSA) undergoes reversible self-aggregation through protein\u2013protein 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\u2022\u2212,\u00a0N3\u2022, SO4\u2022\u2212) with albumin leads to the formation of covalent bonds between tyrosine residues. In the case of \u2022OH radicals and partly, Cl2\u2022\u2212, species other than DT are formed. The light emission of this species is similar to the emission of self-associated HSA.<\/jats:p>","DOI":"10.3390\/ijms23158090","type":"journal-article","created":{"date-parts":[[2022,7,22]],"date-time":"2022-07-22T12:53:45Z","timestamp":1658494425000},"page":"8090","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["Spontaneous and Ionizing Radiation-Induced Aggregation of Human Serum Albumin: Dityrosine as a Fluorescent Probe"],"prefix":"10.3390","volume":"23","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1394-6770","authenticated-orcid":false,"given":"Karolina","family":"Radomska","sequence":"first","affiliation":[{"name":"Institute of Applied Radiation Chemistry, Faculty of Chemistry, Lodz University of Technology, 93-590 Lodz, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2448-7947","authenticated-orcid":false,"given":"Marian","family":"Wolszczak","sequence":"additional","affiliation":[{"name":"Institute of Applied Radiation Chemistry, Faculty of Chemistry, Lodz University of Technology, 93-590 Lodz, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,7,22]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"10606","DOI":"10.1021\/acs.langmuir.7b02463","article-title":"Direct Evidence of Intrinsic Blue Fluorescence from Oligomeric Interfaces of Human Serum Albumin","volume":"33","author":"Bhattacharya","year":"2017","journal-title":"Langmuir"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"14894","DOI":"10.1021\/la5034959","article-title":"Concentration\u2013Dependent Reversible Self\u2013Oligomerization of Serum Albumins through Intermolecular \u03b2\u2013Sheet Formation","volume":"30","author":"Bhattacharya","year":"2014","journal-title":"Langmuir"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1016\/S0167-6881(01)80022-7","article-title":"Radiation chemistry of proteins","volume":"87","year":"2001","journal-title":"Stud. 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