Testing for Ketoprofen Binding to HSA Coated Magnetic Nanoparticles under Normal Conditions and after Oxidative Stress

• Published in: Molecules (Basel, Switzerland) Switzerland), 2020-04, Vol.25 (8), p.1945
• Main Authors: Ziegler-Borowska, Marta, Mylkie, Kinga, Nowak, Pawel, Rybczynski, Patryk, Sikora, Adam, Chelminiak-Dudkiewicz, Dorota, Kaczmarek-Kedziera, Anna
• Format: Article
• Language: English
• Subjects: Albumin; Amino acids; Binding; Binding Sites; Carrier Proteins; Chromatography, High Pressure Liquid; Coated Materials, Biocompatible; Computer simulation; Drug dosages; HSA–drug interaction; Human serum albumin; human serum albumin (HSA); Humans; Hydrogen peroxide; Ketoprofen; Ketoprofen - chemistry; Ligands; Magnetic cores; magnetic nanoparticles; Magnetite Nanoparticles - chemistry; Models, Molecular; Molecular Conformation; Molecular Structure; Nanoparticles; Nonsteroidal anti-inflammatory drugs; Oxidative Stress; Polypeptides; polysaccharide coating; Polysaccharides - chemistry; Protein Binding; Proteins; Serum albumin; Serum Albumin - chemistry; Serum proteins; Sodium; Spectrum analysis; Studies; Sulfur
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules25081945

Binding and transport of ligands is one of the most important functions of human blood serum proteins. Human serum albumin is found in plasma at the highest concentration. Because of this, it is important to study protein-drug interactions for this albumin. Since there is no single model describing this interaction, it is necessary to measure it for each active substance. Drug binding should also be studied in conditions that simulate pathological conditions of the body, i.e., after oxidative stress. Due to this, it is expected that the methods for testing these interactions need to be easy and fast. In this study, albumin immobilized on magnetic nanoparticles was successfully applied in the study of protein-drug binding. Ketoprofen was selected as a model drug and interactions were tested under normal conditions and artificially induced oxidative stress. The quality of obtained results for immobilized protein was confirmed with those for free albumin and literature data. It was shown that the type of magnetic core coverage does not affect the quality of the obtained results. In summary, a new, fast, effective, and universal method for testing protein-drug interactions was proposed, which can be performed in most laboratories.