0000000000465406

AUTHOR

Anna Ploch-jankowska

0000-0001-8480-330x

showing 3 related works from this author

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

2021

Human serum albumin (HSA) is the most abundant human plasma protein. HSA plays a crucial role in many binding endos- and exogenous substances, which affects their pharmacological effect. The innovative aspect of the study is not only the interaction of fatted (HSA) and defatted (dHSA) human serum albumin with ibuprofen (IBU), but the analysis of the influence of temperature on the structural modifications of albumin and the interaction between the drug and proteins from the temperature characteristic of near hypothermia (308 K) to the temperature reflecting inflammation in the body (312 K and 314 K). Ibuprofen is a non-steroidal anti-inflammatory drug. IBU is used to relieve acute pain, inf…

Circular dichroismSerum albuminPharmaceutical ScienceFluorescence spectroscopy03 medical and health scienceschemistry.chemical_compoundPharmacy and materia medicamedicinespectrophotometricibuprofen030304 developmental biology0303 health sciencesChromatographybiologyChemistry030302 biochemistry & molecular biologyAlbuminIbuprofenHuman serum albuminFluorescencecircular dichroismRS1-441spectrofluorometrichuman serum albuminDHSAbiology.proteinmedicine.drugScientia Pharmaceutica
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A Comprehensive Spectroscopic Analysis of the Ibuprofen Binding with Human Serum Albumin, Part I

2020

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, spectrop…

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.drugPharmaceuticals
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The Advances and Challenges of Liposome-Assisted Drug Release in the Presence of Serum Albumin Molecules: The Influence of Surrounding pH

2022

The aim of this study is to prepare a liposomal delivery system for 5-methyl-12 (H)-quino[3,4-b]-1,4-benzothiazine chloride (5-MBT) and study the in vitro release characteristics. The release of 5-MBT from a liposomal complex with human serum albumin (HSA) [LDPPC/5-MBT]:HSA was examined using the spectrophotometric method and differential scanning calorimetry (DSC). Electronic paramagnetic resonance was used to assess the influence of the pH of the environment on the conformation of phospholipids, the latter determining the degree of release of the encapsulated compound. The applied mathematical models made it possible to determine the necessary analytical parameters to facilitate the proce…

biological systems; release mechanism; controlled drug delivery; nanoparticlesrelease mechanismembryonic structuresbiological systemsnanoparticlesGeneral Materials Sciencecontrolled drug deliveryMaterials
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