ArticleThe journal of physical chemistry. B2025
Human Serum Albumin Loaded with Fatty Acids Reveals Complex Protein-Ligand Thermodynamics and Boleadora-Type Solution Dynamics Leading to Gelation.
Article in The journal of physical chemistry. B, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Fatty Acid Deaggregation and Extraction from Vesicles by Serum Albumin Proceeds Via a Dock-and-Load Mechanism.The journal of physical chemistry letters · 2026Article
- Mapping of TEMPO‑, PROXYL‑, and Phosphoryl-Functionalized Spin Probes into Biointerface Fatty Acid Recognition Sites of BSA.ACS omega · 2026Article
- Functional thermodynamics govern the ligand binding to human cytosolic transport proteins.Protein science : a publication of the Protein Society · 2026Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using an electron paramagnetic resonance (EPR) spectroscopic strategy that has been developed for core-shell polymers, the complexity of the binding of fatty acids to human serum albumin (HSA) is characterized in detail. We unravel the internal dynamics of HSA solutions with fatty acids by applying continuous wave EPR (CW EPR) from which we derive a consistent thermodynamic interpretation about fatty acid interactions with HSA in the investigated temperature range of 5-97 °C. Additionally, data from CW EPR are corroborated by dynamic light scattering (DLS), differential scanning calorimetry (DSC) and nanoscale distance measurements using double electron-electron resonance (DEER) spectroscopy. We discuss our data in light of decades of biophysical studies on albumin and aim at drawing a complete functional and dynamic picture of HSA "at work". This picture suggests that HSA is built from modular, rotationally decoupled domains that resemble an entangled three-piece
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