ArticleNaunyn-Schmiedeberg's archives of pharmacology2025
Ligand-human serum albumin analysis: the near-UV CD and UV-Vis spectroscopic studies.
Article in Naunyn-Schmiedeberg's archives of pharmacology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The trial behind it
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Who cites it
4 citing papers in PubMed.
- Spectroscopic and calorimetric analysis of the interaction between human serum albumin and newly synthesized quinoline derivatives.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Human Serum Albumin as a Prodrug Carrier for Tumor Therapy: Mechanisms, Applications, and Future Perspectives.Pharmaceutics · 2026Review
- Hyaluronic Acid-Modified Nanoparticles Loaded with Cabazitaxel: A Promising Nanomedicine for Malignant Prostate Tumors.Current drug delivery · 2026Article
- Improved albumin binding properties of Isoguvacine upon esterification as characterized by biophysical and computational tools.Scientific reports · 2025Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Spectroscopic methods offer many new opportunities to study protein-ligand interactions. The aim of this study was to evaluate the possibility of using near-UV CD as well as UV-Vis spectroscopic techniques to study the interaction between human serum albumin (HSA) and markers of Sudlow's site I (warfarin, phenylbutazone) and II (ketoprofen, ibuprofen), as well as prednisolone and indapamide. In order to perform the planned measurements, near-UV CD spectropolarimetry and UV-Vis spectrophotometry have been used. It has been demonstrated that both techniques allow for rapid evaluation of non-covalent interactions between HSA and ligand, as well as identification of the HSA aromatic amino acid residues involved in this process. The near-UV CD spectroscopic data were more valuable than the analysis based on the second derivative of differential UV-Vis absorption spectra, especially for ligands with a non-specified binding site and low affinity towards HSA, such as prednisolone. The combination of both techniques makes it possible for comprehensive analysis of the interaction between HSA and ligands.
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Registered trials
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