{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T14:12:32Z","timestamp":1789567952981,"version":"build-2803163510"},"reference-count":34,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T00:00:00Z","timestamp":1789516800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pharmaceuticals"],"abstract":"<jats:p>Background: Human serum albumin (HSA) is a critical therapeutic protein with widespread clinical applications. Despite standardised manufacturing protocols, quality variations between HSA preparations are poorly characterised. Objective: To comprehensively characterise five commercial plasma-derived albumin preparations (VIALEBEX\u00ae, ALBUNORM\u00ae, ALBUREX\u00ae, FLEXBUMIN\u00ae, ALBUTEIN\u00ae) using multiple analytical approaches to assess structural integrity, post-translational modifications, functional properties and purity. Methods: Ten batches in total from five manufacturers were analysed using size-exclusion chromatography (SEC) for aggregate quantification, ion exchange chromatography (IEX) for isoform profiling, surface plasmon resonance (SPR) for neonatal Fc receptor (FcRn) binding, and liquid chromatography-tandem mass spectrometry (LC-MS\/MS) for protein quantification. Results: VIALEBEX\u00ae contained the highest proportion of native HSA (35.2% vs. 15.1\u201322.2%) and the lowest levels of oxidised forms (13.2% vs. 27.4\u201333.3%) despite higher polymer content. SPR demonstrated higher FcRn binding affinity for VIALEBEX\u00ae. All preparations exceeded 98% albumin purity, with varying co-purified protein profiles. Conclusions: Significant quality variations exist between HSA preparations. VIALEBEX\u00ae demonstrated greater structural integrity and functional properties despite a higher polymer content, suggesting complex quality relationships beyond simple aggregation. The preservation of structural integrity and higher redox state of VIALEBEX\u00ae could be relevant considerations when selecting a product for clinical or pre-clinical use.<\/jats:p>","DOI":"10.3390\/ph19091470","type":"journal-article","created":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T13:50:27Z","timestamp":1789566627000},"page":"1470","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Comparative Characterisation of Five Plasma-Derived Human Serum Albumin Preparations: Structural Integrity, Functional Properties, and Quality Attributes"],"prefix":"10.3390","volume":"19","author":[{"given":"Zeineb","family":"Farhane","sequence":"first","affiliation":[{"name":"LFB Biotechnologies, 91940 Les Ulis, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Melanie","family":"Bilong","sequence":"additional","affiliation":[{"name":"LFB Biotechnologies, 91940 Les Ulis, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maud","family":"Le Boedec","sequence":"additional","affiliation":[{"name":"LFB Biotechnologies, 91940 Les Ulis, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Victor","family":"Blanchard","sequence":"additional","affiliation":[{"name":"LFB Biotechnologies, 91940 Les Ulis, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arthur","family":"Besle","sequence":"additional","affiliation":[{"name":"LFB Biotechnologies, 91940 Les Ulis, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nolwenn","family":"Tilly","sequence":"additional","affiliation":[{"name":"LFB Biotechnologies, 91940 Les Ulis, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander","family":"Seifert","sequence":"additional","affiliation":[{"name":"LFB Biotechnologies, 91940 Les Ulis, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,9,16]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"462240","DOI":"10.1016\/j.chroma.2021.462240","article-title":"Characterization of drug binding with alpha(1)-acid glycoprotein in clinical samples using ultrafast affinity extraction","volume":"1649","author":"Beeram","year":"2021","journal-title":"J. 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