2024/09/30 by Wojciech Rogóż, Aleksandra Owczarzy, Karolina Kulig +1
Biochemistry, Genetics and Molecular Biology · Medicine · #Antibiotics Pharmacokinetics and Efficacy #Hemoglobin structure and function #Protein Interaction Studies and Fluorescence Analysis
paper · pdf · doi:10.1007/s00210-024-03471-3
crossref issued 2024/09/30 · crossref published 2024/09/30 · crossref published-online 2024/09/30 · openalex publication_date 2024/09/30 · crossref created 2024/09/30 · crossref published-print 2025/03/01 · crossref deposited 2025/03/18 · openalex created_date 2025/10/10 · crossref indexed 2026/07/31 · openalex updated_date 2026/07/31
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.