Search results for "Binding constant"

showing 10 items of 47 documents

Interaction of Quinine with Model Lipid Membranes of Different Compositions

2002

The binding of a drug such as Quinine with neutral and negatively charged small unilamellar lipid vesicles at pH 7 and 37 degrees C was investigated. Changes in the fluorescence properties of the drug after association with the liposomes were used to obtain binding isotherms over a range of phospholipid compositions at different ionic strengths. Under such conditions, the association was strongly enhanced by the negative net charge of the bilayer but diminished by the increasing presence of electrolytes in the aqueous media. Binding data were analyzed in terms of a surface partition equilibrium without and after correcting for electrostatic effects by means of the Gouy-Chapman theory. The i…

LiposomeBinding SitesChromatographyQuinineChemistryBilayerLipid BilayersStatic ElectricityPhospholipidPharmaceutical ScienceMembranes ArtificialPhosphatidylglycerolsBinding constantPartition coefficientHydrophobic effectchemistry.chemical_compoundIonic strengthPartition equilibriumBiophysicsJournal of Pharmaceutical Sciences
researchProduct

Binding of urate and caffeine to hemocyanin of the lobster Homarus vulgaris (E.) as studied by isothermal titration calorimetry.

2000

Hemocyanin serves as an oxygen carrier in the hemolymph of the European lobster Homarus vulgaris. The oxygen binding behavior of the pigment is modulated by metabolic effectors such as lactate and urate. Urate and caffeine binding to 12-meric hemocyanin (H. vulgaris) was studied using isothermal titration calorimetry (ITC). Binding isotherms were determined for fully oxygenated hemocyanin between pH 7.55 and 8.15. No pH dependence of the binding parameters could be found for either effector. Since the magnitude of the Bohr effect depends on the urate concentration, the absence of any pH dependence of urate and caffeine binding to oxygenated hemocyanin suggests two conformations of the pigme…

Malemedicine.medical_treatmentBohr effectBuffersCalorimetryBiochemistryCaffeineHemolymphmedicineAnimalsBinding siteTromethamineBinding SitesChemistryTitrimetryIsothermal titration calorimetryHemocyaninHydrogen-Ion ConcentrationBinding constantNephropidaeUric AcidCrystallographyHemocyaninsThermodynamicsTitrationOxygen bindingBiochemistry
researchProduct

G-quadruplex vs. duplex-DNA binding of nickel(II) and zinc(II) Schiff base complexes

2016

Novel nickel(II) (1) and zinc(II) (2) complexes of a Salen-like ligand, carrying a pyrimidine ring on the N,N' bridge, were synthesized and characterized. Their interaction with duplex and G-quadruplex DNA was investigated in aqueous solution through UV-visible absorption, circular dichroism and viscometry measurements. The results obtained point out that, while the zinc(II) complex does not interact with both duplex and G-quadruplex DNA, the nickel(II) complex 1 binds preferentially to G-quadruplex respect to duplex-DNA, with values of the DNA-binding constants, Kb, 2.6×10(5)M(-1) and 3.5×10(4)M(-1), respectively. Molecular dynamics simulations provided an atomic level model of the top-sta…

Models MolecularCircular dichroismComputational chemistryInorganic chemistryBinding constantchemistry.chemical_elementZincCircular dichroism010402 general chemistryG-quadruplexDNA G-quadruplex nickel01 natural sciencesBiochemistryInorganic Chemistrychemistry.chemical_compoundNickelheterocyclic compoundsSchiff BasesSchiff base010405 organic chemistryOligonucleotidezincDNABinding constantSettore CHIM/08 - Chimica Farmaceutica0104 chemical sciencesG-QuadruplexesCrystallographyNickelchemistryDuplex (building)Settore CHIM/03 - Chimica Generale E Inorganica
researchProduct

Synthesis, characterization, cellular uptake and interaction with native DNA of a bis(pyridyl)-1,2,4-oxadiazole copper(II) complex

2010

The copper(II) complex of 3,5-bis(2'-pyridyl)-1,2,4-oxadiazole was synthesized and characterized. X-Ray crystallography revealed that the complex consists of a discrete [Cu(3,5-bis(2'-pyridyl)-1,2,4-oxadiazole)(2)(H(2)O)(2)](2+) cation and two ClO(4)(-) anions. The Cu(II) coordination sphere has a distorted octahedral geometry and each ligand chelates the copper ion through the N(4) nitrogen of the oxadiazole ring and the nitrogen of one pyridine moiety. The coordinated water molecules are in cis position and each of them is H-bonded to the 5-pyridyl nitrogen of the oxadiazole ligand and to an oxygen of the perchlorate anion. Biological assays showed that, despite the free ligand not being …

Models MolecularCircular dichroismCoordination sphereheterocylces metal complex DNA binders anti-tumoralsCell SurvivalPyridinesStereochemistrychemistry.chemical_elementOxadiazoleLigandsInorganic Chemistrychemistry.chemical_compoundPerchlorateCell Line TumorOctahedral molecular geometryOrganometallic CompoundsHumansOxadiazolesChemistryLigandDNASettore CHIM/06 - Chimica OrganicaCopperBinding constantCrystallographySettore CHIM/03 - Chimica Generale E InorganicaCopper
researchProduct

Two copper complexes from two novel naphthalene-sulfonyl-triazole ligands: different nuclearity and different DNA binding and cleavage capabilities.

2013

[EN] Two novel naphthalene-sulfonyl-triazole ligands, 5-amino-N1-(naphthalen-3-ylsulfony1)-1,2,4-triazole (anstrz) and 3,5-diamino-N1-(naphthalen-3-ylsulfony1)-1,2,4-triazole (danstrz), purposely designed to interact with DNA, have been prepared for the first time and then fully characterized by H-1, C-13 NMR and IR spectroscopy, mass spectrometry and elemental analysis. The crystal structures of two copper complexes of these derivatives, i.e. [Cu(anstrz)(4)(NO3)(2)]center dot 4CH(3)OH (1), mononuclear, and [Cu(danstrz)(mu-OAc)(2)](2)center dot 2(danstrz) (OAc = acetato) (2), dinuclear, have been determined by single-crystal X-ray diffraction. In both cases the ligand coordinates in a monod…

Models MolecularDenticity124-Triazole ligandsStereochemistryTriazolePaddle wheel type copper acetate compoundCrystal structureNaphthalenesCrystallography X-RayLigandsBiochemistryInorganic Chemistrychemistry.chemical_compoundX-Ray DiffractionCoordination ComplexesBIOQUIMICA Y BIOLOGIA MOLECULARSulfonesBinding siteDNA CleavageCu(II)-triazole complexesBond cleavageNuclease activitySulfonylchemistry.chemical_classificationSulfonamidesBinding SitesDeoxyribonucleasesChemistryLigandDNATriazolesBinding constantDNA interactionCrystallographyCopperJournal of inorganic biochemistry
researchProduct

Formation of irreversibly bound annexin A1 protein domains on POPC/POPS solid supported membranes

2008

AbstractThe specific interaction of annexin A1 with phospholipid bilayers is scrutinized by means of scanning force and fluorescence microscopy, quartz crystal microbalance, ellipsometry, and modeled by dynamic Monte Carlo simulations. It was found that POPC/POPS bilayers exhibit phase separation in POPC- and POPS-enriched domains as a function of Ca2+ concentration. Annexin A1 interacts with POPC/POPS bilayers by forming irreversibly bound protein domains with monolayer thickness on POPS-enriched nanodomains, while the attachment of proteins to the POPC-enriched regions is fully reversible. A thorough kinetic analysis of the process reveals that both, the binding constant of annexin A1 at …

Models Moleculargenetic structuresLipid BilayersBiophysicsPhospholipidAnalytical chemistryPhosphatidylserines02 engineering and technologyMicroscopy Atomic ForceBiochemistryBiophysical PhenomenaMembrane Lipids03 medical and health scienceschemistry.chemical_compoundProtein structureSFMMonolayerMicropatterned membranesAnimalsHumansPOPCMonte Carlo simulationAnnexin A1030304 developmental biologyFluorescence microscopy0303 health sciencesEllipsometrytechnology industry and agricultureCell BiologyQuartz crystal microbalanceSurface Plasmon Resonance021001 nanoscience & nanotechnologyBinding constantProtein Structure TertiaryMembraneMicroscopy FluorescencechemistryQCMPhosphatidylcholinesBiophysicsCalciumlipids (amino acids peptides and proteins)Adsorption0210 nano-technologyMonte Carlo MethodProtein BindingAnnexin A1Biochimica et Biophysica Acta (BBA) - Biomembranes
researchProduct

Reversible Dioxygen Binding and Phenol Oxygenation in a Tyrosinase Model System

2000

The complex [Cu2(L-66)]2+ (L-66 = a,a'-bis¿bis[2-(1'-methyl-2'-benzimidazolyl)ethyl]amino¿-m-xylene) undergoes fully reversible oxygenation at low temperature in acetone. The optical [lambda(max) = 362 (epsilon 15000), 455 (epsilon 2000), and 550 nm (epsilon 900M(-1)cm(-1))] and resonance Raman features (760 cm(-1), shifted to 719cm(-1)(-1) with 18O2) of the dioxygen adduct [Cu2(L-66)(O2)]2+ indicate that it is a mu-eta2:eta2-peroxodicopper(II) complex. The kinetics of dioxygen binding, studied at - 78 degrees C, gave the rate constant k1 = 1.1M(-1) 5(-1) for adduct formation, and k(-1) =7.8 x 10(-5)s(-1), for dioxygen release from the Cu2O2 complex. From these values, the O2 binding consta…

Monophenol MonooxygenaseChemistrySpectrophotometry AtomicTyrosinaseOrganic ChemistryKineticsGeneral ChemistryResonance (chemistry)PhotochemistryMedicinal chemistryBinding constantCatalysisQuinoneAdductOxygenchemistry.chemical_compoundReaction rate constantModels ChemicalPhenolsAcetoneOxidation-ReductionChemistry - A European Journal
researchProduct

DNA Binding Studies and Cytotoxicity of a Dinuclear PtII Diazapyrenium- Based Metallo-supramolecular Rectangular Box

2012

The interaction with native DNA of a 2,7-diazapyrenium-based ligand 1 and its Pt II rectangular metal- lacycle 2 is explored through circular and linear dichroism and fluorescence spectroscopies. The metal-free ligand 1 binds through intercalation, with a binding constant of approximately 5 � 10 5 m � 1 , whereas the metallacycle 2 binds and bends the DNA with a bind- ing constant of 7 � 10 6 m � 1 . PCR assays show that metallo-supramolecular box 2 interferes with DNA transactions in vitro whereas the intercalator 1 does not. The metallacycle is active against four human cancer cell lines, with IC50 values ranging between 3.1 and 19.2 mm and shows similar levels of efficacy, but a differen…

Organoplatinum CompoundsCell SurvivalStereochemistryIntercalation (chemistry)Molecular ConformationSupramolecular chemistryAntineoplastic AgentsApoptosisLigandsNucleic Acid DenaturationLinear dichroismCatalysissupramolecular chemistryInhibitory Concentration 50chemistry.chemical_compoundCell Line TumorSettore BIO/10 - BiochimicaHumansmetallodrugPlatinumnoncovalent DNA bindingChemistryCircular DichroismOrganic ChemistryDNA NeoplasmGeneral ChemistrySettore CHIM/06 - Chimica OrganicaMetallacycleLigand (biochemistry)Binding constantFluorescenceSettore CHIM/08 - Chimica FarmaceuticaIntercalating AgentsKineticsSpectrometry FluorescenceSettore CHIM/03 - Chimica Generale E InorganicaThermodynamicscytotoxicityPtII rectangular boxCisplatinDNAPhenanthrolines
researchProduct

Peculiar mechanism of solubilization of a sparingly water soluble drug into polymeric micelles. Kinetic and equilibrium studies.

2012

Complementary kinetic and equilibrium studies on the solubilization process of the sparingly water soluble tamoxifen (TAM) drug in polymeric aqueous solutions have been performed by using the spectrophotometric method. In particular, the amphiphilic copolymers obtained by derivatization of polymeric chain of poly(N-2-hydroxyethyl)-dl-aspartamide, PHEA, with poly(ethylene glycol)s, PEG (2000 or 5000 Da), and/or hexadecylamine chain, C16, namely PHEA-PEG2000-C16, PHEA-PEG5000-C16, PHEA-C16, have been employed. Preliminary to the kinetic and equilibrium data quantitative treatment, the molar absorption coefficient of TAM in polymeric micelle aqueous solution has been determined. By these studi…

PolymersSurface PropertiesKineticsMicellesparingly water soluble drug TAM polymeric micelle kineticchemistry.chemical_compoundReaction rate constantstomatognathic systemMaterials ChemistryCopolymerOrganic chemistryPhysical and Theoretical ChemistrySolubilityParticle SizeMicellesSettore CHIM/02 - Chimica FisicaAqueous solutionWaterBinding constantSurfaces Coatings and FilmsKineticsTamoxifenchemistryChemical engineeringSolubilityEthylene glycolThe journal of physical chemistry. B
researchProduct

Analysis of mebendazole binding to its target biomolecule by laser flash photolysis

2016

[EN] Mebendazole (MBZ) and related anticancer benzimidazoles act binding the beta-subunit of Tubulin (TU) before dimerization with alpha-TU with subsequent blocking microtubule formation. Laser flash photolysis (LFP) is a new tool to investigate drug-albumin interactions and to determine binding parameters such as affinity constant or population of binding sites. The aim of this study was to evaluate the interactions between the nonfluorescent mebendazole (MBZ) and its target biomolecule TU using this technique. Before analyzing the MBZ@TU complex it was needed to determine the photophysical properties of MBZ triplet excited state ((3)MBZ*) in different media. Hence, 3MBZ* showed a transien…

PopulationBiophysicsBinding constantElectron donor010402 general chemistryPhotochemistry01 natural sciencesAnticancer drugschemistry.chemical_compoundQUIMICA ORGANICAMebendazole triplet excited stateTubulinUltrafast laser spectroscopyRadiology Nuclear Medicine and imagingeducationchemistry.chemical_classificationeducation.field_of_studyRadiationPhotolysisRadiological and Ultrasound Technology010405 organic chemistryPhosphorescenceLasersPhotodissociationTemperatureLaser flash photolysisElectron acceptorBinding constant0104 chemical sciencesMebendazolechemistryExcited stateFlash photolysisThermodynamicsSpectrophotometry UltravioletProtein Binding
researchProduct