Search results for "binding"

showing 10 items of 3896 documents

Role of Seroalbumin in the Cytotoxicity of cis-Dichloro Pt(II) Complexes with (N^N)-Donor Ligands Bearing Functionalized Tails

2018

Given the potent anticancer properties of cisdiamminedichloroplatinum( II) and knowing its mode of action, we synthesized four new cis-[PtCl2(N^N)] organoplatinum complexes, two with N-substituted pbi ligands (pbiR = 1-R-2-(2-pyridyl)benzimidazole) (namely, 1 and 2) and two more with 4,4′-disubstituted bpy ligands (bpy = 2,2′-bipyridine) (namely, 3 and 4). We explored their cytotoxicity and ability to bind to deoxyguanosine monophosphate (dGMP), DNA, and albumin models. By 1H NMR and UV−vis spectroscopies, circular dichroism, agarose gel electrophoresis, differential scanning calorimetry measurements, and density functional theory calculations, we verified that only 3 can form aquacomplex s…

Circular dichroismCell SurvivalStereochemistryLigandPlasma protein bindingHeLa CellLigands010402 general chemistry01 natural sciencesChemistry Physical and theoreticalInorganic ChemistryHeLaBipyridinechemistry.chemical_compoundDrug StabilityCoordination ComplexesQuímica físicaHumansPhysical and Theoretical ChemistryCytotoxicityA549 CellOrganoplatinumPlatinumCoordination ComplexeCalorimetry Differential ScanningMolecular Structurebiology010405 organic chemistryChemistryRational designDeoxyguanine NucleotidesSerum Albumin BovineDNAbiology.organism_classification0104 chemical sciencesSettore CHIM/03 - Chimica Generale E InorganicaA549 CellsAgarose gel electrophoresisDeoxyguanine NucleotideHumanHeLa CellsProtein BindingInorganic Chemistry
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Optical studies on interaction of biliary contrast agents with native and modified human serum albumin.

1981

The interaction of two homologous series of biliary contrast agents with native human and bovine serum albumin and with modified human serum albumin was investigated using circular dichroism and equilibrium dialysis. For most derivatives, extrinsic Cotton effects were observed for the interaction with both albumins. In some cases, these effects were strongly affected by only small changes in the chemical structure of the drugs. These large differences in extrinsic Cotton effects can be explained by definite effects of the chemical structures on the binding site selectivity of some drugs. For example, iopodate preferentially binds to the warfarin binding site of human Scrum albumin, while an…

Circular dichroismChemical PhenomenaSerum albuminPharmaceutical ScienceContrast MediaPlasma protein bindingmedicineAnimalsHumansBovine serum albuminBinding siteBiliary TractSerum AlbuminDiazepam bindingbiologyChemistryCircular DichroismAlbuminTryptophanSerum Albumin BovineHuman serum albuminRadiographyChemistryBiochemistrybiology.proteinTyrosineCattleDialysismedicine.drugProtein BindingJournal of pharmaceutical sciences
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Optical studies on the specific interaction of dipyridamole with alpha 1-acid glycoprotein (orosomucoid).

1982

Abstract The interaction of dipyridamole with α1-acid glycoprotein was investigated by circular dichroism and ultraviolet absorbance measurements as well as by equilibrium dialysis experiments. Dipyridamole is bound to the protein via one site of extremely high affinity and by at least one site of considerably lower affinity. Only the association of dipyridamole with the high affinity site produces typical extrinsic Cotton effects. As a result of experimental observations it is concluded that the high affinity site is located in a hydrophobic protein structure of the glycoprotein.

Circular dichroismChemical PhenomenaStereochemistryProtein ConformationPharmaceutical ScienceOrosomucoidIn Vitro TechniquesProtein structuremedicineHumansPharmacologychemistry.chemical_classificationbiologyChemistry PhysicalCircular DichroismTryptophanDipyridamoleOrosomucoidUltraviolet absorbanceDipyridamoleLower affinitychemistryα1 acid glycoproteinbiology.proteinTyrosineSpectrophotometry UltravioletGlycoproteinDialysismedicine.drugProtein BindingThe Journal of pharmacy and pharmacology
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The interaction of Schiff Base complexes of nickel(II) and zinc(II) with duplex and G-quadruplex DNA

2017

The duplex and G-quadruplex DNA-binding of six nickel(II) and zinc(II) complexes of three salphen-like ligands (salphen = N,N?-bis-salicylidene-1,2-phenylenediaminato) was investigated by UV-visible absorption and circular dichroism spectroscopy. The results obtained, in particular the values of the DNA-binding constants, Kb, point out that the nickel(II) complexes show a higher affinity toward both duplex and G-quadruplex DNA, compared to the analogous zinc(II) complexes. Interestingly, the zinc(II) complexes possess high selectivity toward G-quadruplex DNA, being negligible their binding with duplex DNA. Molecular dynamics (MD) simulations provided atomistic models for the interpretation …

Circular dichroismComputational chemistryInorganic chemistryBinding constantchemistry.chemical_element-Zinc010402 general chemistryG-quadruplex01 natural sciencesBiochemistryInorganic Chemistrychemistry.chemical_compoundCoordination ComplexesNickelheterocyclic compoundsSchiff BasesSchiff baseG-quadruplex010405 organic chemistryDNABinding constant0104 chemical sciencesG-QuadruplexesNickelCrystallographyZincchemistryDuplex (building)Settore CHIM/03 - Chimica Generale E InorganicaDNA
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The interaction of native calf thymus DNA with FeIII-dipyrido[3,2-a:2’,3’-c]phenazine

2008

The mono and bis dipyrido[3,2-a:2',3'-c]phenazine (dppz) adducts of iron(III) chloride, i.e. [Fe(dppz)]Cl(3) and [Fe(dppz)(2)]Cl(3), have been synthesized and characterized. The interaction of the Fe(III)dppz hydrolyzed aquo complex with native calf thymus DNA has been monitored as a function of the metal complex-DNA molar ratio, by variable temperature UV absorption spectrophotometry, circular dichroism (CD) and fluorescence spectroscopy. The results obtained in solution at various ionic strength values give support for a tight intercalative binding of the Fe(III)dppz cation with DNA. In particular, the appearance of induced CD bands, caused by the addition of Fe(III)dppz, indicate the exi…

Circular dichroismDNA dppz Intercalation Iron SpectroscopyIntercalation (chemistry)PhenazinePhotochemistryNucleic Acid DenaturationBiochemistryFerric CompoundsFluorescenceAdductInorganic ChemistryMetalchemistry.chemical_compoundDNA AdductsMetal aquo complexChemistryCircular DichroismDNABinding constantCrystallographyIonic strengthSettore CHIM/03 - Chimica Generale E Inorganicavisual_artvisual_art.visual_art_mediumPhenazines
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Spectroscopic and electrochemical study of interactions between DNA and different salts of 1,4-dihydropyridine AV-153

2020

1,4-dihydropyridines (1,4-DHP) possess important biochemical and pharmacological properties, including antimutagenic and DNA-binding activity. The latter activity was first described for water-soluble 1,4-DHP with carboxylic group in position 4, the sodium salt of the 1,4-DHP derivative AV-153 among others. Some data show the modification of physicochemical properties and biological activities of organic compounds by metal ions that form the salts. We demonstrated the different affinity to DNA and DNA-protecting capacity of AV-153 salts, depending on the salt-forming ion (Na, K, Li, Rb, Ca, Mg). This study aimed to use different approaches to collate data on the DNA-binding mode of AV-153-N…

Circular dichroismGuanine030303 biophysicsIntercalation (chemistry)Biophysicslcsh:MedicineCircular dichroismG-quadruplexBiochemistryMedicinal chemistryGeneral Biochemistry Genetics and Molecular BiologyNucleobase03 medical and health scienceschemistry.chemical_compoundCircular voltammetryMoleculeDenaturation (biochemistry)DNA bindingMolecular Biology14-dihydropyridines030304 developmental biologyAV-153 salts0303 health sciencesGeneral Neurosciencelcsh:RGeneral MedicineG-quadruplexeschemistryFourier-transformed infrared spectroscopySpectrofluorimetryGeneral Agricultural and Biological SciencesDNAPeerJ
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The interaction of native DNA with Zn(II) and Cu(II) complexes of 5-triethyl ammonium methyl salicylidene orto-phenylendiimine

2007

The interaction of native calf thymus DNA with the Zn(II) and Cu(II) complexes of 5-triethyl ammonium methyl salicylidene orto-phenylendiimine (ZnL(2+) and CuL(2+)), in 1 mM Tris-HCl aqueous solutions at neutral pH, has been monitored as a function of the metal complex-DNA molar ratio by UV absorption spectrophotometry, circular dichroism (CD) and fluorescence spectroscopy. The results support for an intercalative interaction of both ZnL(2+) and CuL(2+) with DNA, showing CuL(2+) an affinity of approximately 10 times higher than ZnL(2+). In particular, the values of the binding constant, determined by UV spectrophotometric titration, equal to 7.3x10(4) and 1.3x10(6)M(-1), for ZnL(2+) and CuL…

Circular dichroismInorganic chemistrychemistry.chemical_elementZincNucleic Acid DenaturationBiochemistryFluorescence spectroscopyInorganic ChemistryMetalSchiff baseOrganometallic CompoundsIntercalationAnimalsQualitative inorganic analysisSchiff BasesAqueous solutionQuenching (fluorescence)ChemistryCircular DichroismDNASettore CHIM/06 - Chimica OrganicaBinding constantQuaternary Ammonium CompoundsCrystallographyZincSettore CHIM/03 - Chimica Generale E Inorganicavisual_artvisual_art.visual_art_mediumCattleSpectrophotometry UltravioletIminesCopper
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Influence of pH on the benzodiazepine-human serum albumin complex. Circular dichroism studies.

1974

The influence of pH on the binding of benzodiazepine derivatives to HSA was studied by circular dichroism measurements and by gel filtration. The binding of nearly all benzodiazepines is increased by rising the pH from 6.60 to 8.20. For flurazepam, clonazepam, and nitrazepam this increase in binding is due to an increase of the affinities, while for the other substances the affinity remains constant and the number of binding sites is increased from one to two. The changes in binding of the benzodiazepines by rising the pH are explained by a cationic amino acid residue near or at the benzodiazepine binding site of the HSA molecule. This second binding site is not detectable by circular dichr…

Circular dichroismNitrazepamChemical Phenomenamedicine.drug_classStereochemistryFlurazepamSize-exclusion chromatographyPlasma protein bindingFlurazepammedicineHumansBinding siteNitrazepamSerum AlbuminPharmacologyBenzodiazepineBenzodiazepinonesBinding SitesDiazepamChemistryOxazepamCircular DichroismOsmolar ConcentrationChlordiazepoxideGeneral MedicineBenzazepinesHydrogen-Ion ConcentrationHuman serum albuminChemistryKineticsBiophysicsmedicine.drugProtein BindingNaunyn-Schmiedeberg's archives of pharmacology
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Characterization of the interaction between Actinin-Associated LIM Protein (ALP) and the rod domain of α-actinin

2009

Abstract Background The PDZ-LIM proteins are a family of signalling adaptors that interact with the actin cross-linking protein, α-actinin, via their PDZ domains or via internal regions between the PDZ and LIM domains. Three of the PDZ-LIM proteins have a conserved 26-residue ZM motif in the internal region, but the structure of the internal region is unknown. Results In this study, using circular dichroism and nuclear magnetic resonance (NMR), we showed that the ALP internal region (residues 107–273) was largely unfolded in solution, but was able to interact with the α-actinin rod domain in vitro, and to co-localize with α-actinin on stress fibres in vivo. NMR analysis revealed that the ti…

Circular dichroismPDZ domaineducationAmino Acid MotifsMolecular Sequence DataPlasma protein bindingActininmacromolecular substancesBiology03 medical and health sciences0302 clinical medicineCell Line TumorHumansActininAmino Acid Sequencelcsh:QH573-671Peptide sequenceActin030304 developmental biologyLIM domainFluorescent Dyes0303 health scienceslcsh:CytologyMicrofilament ProteinsCell BiologyLIM Domain ProteinsSurface Plasmon Resonancemusculoskeletal systemRecombinant ProteinsCell biologyProtein Structure TertiaryLHX3Peptides030217 neurology & neurosurgeryResearch ArticleProtein BindingBMC Cell Biology
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Supramolecular Chirogenesis in Bis-Porphyrin: Crystallographic Structure and CD Spectra for a Complex with a Chiral Guanidine Derivative

2021

The complexation of (3aR,7aR)-N-(3,5-bis(trifluoromethyl)phenyl)octahydro-2H-benzo[d]imidazol-2-imine (BTI), as a guest, to ethane-bridged bis(zinc octaethylporphyrin), bis(ZnOEP), as a host, has been studied by means of ultraviolet-visible (UV-Vis) and circular dichroism (CD) absorption spectroscopies, single crystal X-ray diffraction, and computational simulation. The formation of 1:2 host-guest complex was established by X-ray diffraction and UV-Vis titration studies. Two guest BTI molecules are located at the opposite sides of two porphyrin subunits of bis(ZnOEP) host, which is resting in the anti-conformation. The complexation of BTI molecules proceed via coordination of the imine nitr…

Circular dichroismPhysics and Astronomy (miscellaneous)General MathematicsImineSupramolecular chemistrychiralityCrystal structurehost-guest binding010402 general chemistryguanidine01 natural sciencesDFTsupramolecular chemistrykemialliset sidoksetchemistry.chemical_compoundsupramolekulaarinen kemiaComputer Science (miscellaneous)Molecule[CHIM]Chemical SciencesGuanidine010405 organic chemistrylcsh:Mathematicstiheysfunktionaaliteoriahost–guest bindinglcsh:QA1-939Porphyrin0104 chemical sciencescircular dichroismCrystallographyTD-DFT simulationchemistryChemistry (miscellaneous)Chirality (chemistry)porphyrin
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