Search results for "Protein solution"

showing 3 items of 3 documents

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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Intermolecular interactions in metastable protein solutions.

2011

Intermolecular interactionmetastable protein solutions.Settore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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PREDICTION OF THERMODYNAMIC INSTABILITIES OF PROTEIN SOLUTIONS FROM SIMPLE PROTEIN-PROTEIN INTERACTIONS

2013

Statistical thermodynamics of protein solutions is often studied in terms of simple, microscopic models of particles interacting via pairwise potentials. Such modelling can reproduce the short range structure of protein solutions at equilibrium and predict thermodynamics instabilities of these systems. We introduce a square well model of effective protein-protein interaction that embeds the solvent's action. We modify an existing model [45] by considering a well depth having an explicit dependence on temperature, i.e. an explicit free energy character, thus encompassing the statistically relevant configurations of solvent molecules around proteins. We choose protein solutions exhibiting dem…

Quantitative Biology::BiomoleculesSpinodalRange (particle radiation)Liquid–liquid demixingSpinodal lineChemistrySolvent mediated protein-protein interactionEnthalpyProtein solutionGeneral Physics and AstronomyThermodynamicsEntropy driven phase transitionLiquid-liquid demixingAction (physics)Settore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Solvent mediated protein–protein interactionProtein–protein interactionSpinodal lines SW potential free energy parametrizationPhysics and Astronomy (all)Mean field theoryFinite potential wellMoleculePhysical and Theoretical ChemistrySquare well potential
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