6533b822fe1ef96bd127d80b

RESEARCH PRODUCT

A Comprehensive Spectroscopic Analysis of the Ibuprofen Binding with Human Serum Albumin, Part I

Danuta PentakAnna Ploch-jankowska

subject

0301 basic medicinePain reliefPharmaceutical Sciencelcsh:Medicinelcsh:RS1-441030226 pharmacology & pharmacyArticlelcsh:Pharmacy and materia medica03 medical and health sciences0302 clinical medicinespectrofluorometric analysesDrug DiscoverymedicinespectrophotometricSpectroscopyibuprofenScatchard plotChromatographyChemistrylcsh:RHuman serum albuminIbuprofenFluorescenceibuprofen; human serum albumin; spectrophotometric; spectrofluorometric analysesProtein solutionbody regions030104 developmental biologyhuman serum albuminembryonic structuresMolecular Medicinemedicine.drug

description

Human serum albumin (HSA) plays a fundamental role in the human body. It takes part in the transport of exogenic and endogenic substances, especially drugs. Ibuprofen (IBU) is one of the most commonly used non-steroidal anti-inflammatory drugs, used for pain relief, fever relief, and for anti-inflammatory purposes. The binding of ligands with HSA is a significant factor which determines the toxicity and the therapeutic dosages of these substances. The aim of this study was to compare the degree of ibuprofen binding with human serum albumin at various temperatures and protein solution pH values. In order to evaluate conformational changes in HSA caused by interaction with ibuprofen, spectrophotometric (first and second derivatives of the UV-VIS spectrum), and spectrofluorometric analyses were performed concerning the mutual interactions of IBU-HSA. The use of fluorescent spectroscopy allowed for recording fluorescent emissive spectra of HSA (5 &times

yearjournalcountryeditionlanguage
2020-08-21Pharmaceuticals
10.3390/ph13090205http://dx.doi.org/10.3390/ph13090205