Faculty of Chemistry, Nicolaus Copernicus University in Torun, Gagarina 7, 87-100 Torun, Poland.
Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Torun, dr A. Jurasza 2, 85-089 Bydgoszcz, Poland.
Molecules. 2020 Apr 22;25(8):1945. 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.
配体的结合和转运是人体血清蛋白的最重要功能之一。人血清白蛋白在血浆中的浓度最高。因此,研究这种白蛋白的蛋白-药物相互作用很重要。由于没有单一的模型可以描述这种相互作用,因此有必要针对每种活性物质进行测量。还应在模拟体内病理条件的条件下(即氧化应激后)研究药物结合。因此,预计这些相互作用的测试方法需要简单快捷。在这项研究中,成功地将固定在磁性纳米颗粒上的白蛋白应用于研究蛋白-药物结合。选择酮洛芬作为模型药物,并在正常条件和人工诱导的氧化应激下测试相互作用。通过与游离白蛋白和文献数据的结果进行比较,证实了固定化蛋白获得结果的质量。结果表明,磁核覆盖率的类型不影响获得结果的质量。总之,提出了一种新的、快速、有效和通用的蛋白-药物相互作用测试方法,该方法可在大多数实验室中进行。