Search results for "Calorimetry"

showing 10 items of 504 documents

Crystallization, spectral, crystallographical, and thermoanalytical studies of succinobucol polymorphism.

2011

Four different polymorphs, A, C, D, and E, of succinobucol were isolated and characterized by means of solid-state nuclear magnetic resonance spectroscopy, single crystal and powder X-ray diffraction, differential scanning calorimetry, thermogravimetry, and attenuated total reflection–infrared spectroscopy. From a number of experiments, the same polymorphs (C, D, and E) and an equilibrium phase mixture B consisting of polymorphs C and D were repeatedly gained using different solvents or their mixtures. Although polymorph A was obtained directly from recrystallization only on few occasions, polymorphs C, D, and E proved to be metastable kinetic polymorphs, which slowly transform to a thermod…

Models MolecularMagnetic Resonance SpectroscopyCalorimetry Differential ScanningSpectrophotometry InfraredChemistryPharmaceutical ScienceNuclear magnetic resonance spectroscopyCrystallography X-Raylaw.inventionThermogravimetryCrystallographyDifferential scanning calorimetryProbucolPolymorphism (materials science)Solid-state nuclear magnetic resonancelawThermogravimetryCrystallizationCrystallizationta116Single crystalPowder diffractionPowder DiffractionJournal of pharmaceutical sciences
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Structural studies of five novel bile acid-4-aminopyridine conjugates

2012

Abstract Synthesis and solid-state structural characterization of five bile acid amides of 4-aminopyridine (4-AP) are reported. Systematic crystallization experiments revealed a number of structural modifications and/or solvate/hydrate systems for these conjugates. Particularly, cholic acid conjugate exhibited five distinct structure modifications, including one anhydrous form, mono- and dihydrates, as well as ethanol and 2-butanol solvates. The obtained crystal forms were examined extensively with various analytical methods, including solid-state NMR, Raman, and IR spectroscopies, powder and single crystal X-ray diffraction methods, thermogravimetry, and differential scanning calorimetry. …

Models MolecularMagnetic Resonance Spectroscopymedicine.drug_classButanolsClinical BiochemistryCrystallography X-RaySpectrum Analysis RamanBiochemistrylaw.inventionBile Acids and Saltschemistry.chemical_compoundEndocrinologylawmedicineOrganic chemistry4-AminopyridineCrystallizationta116Molecular BiologyPharmacologyCalorimetry Differential ScanningEthanolBile acidOrganic ChemistryCholic acidAmidesThermogravimetryCrystallographychemistryPolymorphism (materials science)ThermogravimetrySolventsCrystallizationHydrateSingle crystalConjugateSteroids
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Structural, Thermoanalytical and Molecular Modeling Studies on N-(3-hydroxypropyl) 3a,12a-Dihydroxy-5b-cholan-24-amide and Its Monohydrates

2007

The synthetic method for preparing N-(3-hydroxypropyl) 3 alpha,12 alpha-dihydroxy-5 beta-cholan-24-amide can lead to formation of at least three different crystal forms - an anhydrous compound and two monohydrates. The structural and thermal properties of these forms have been characterized by 13C-CP/MAS-NMR and IR spectroscopy, thermo- gravimetry, differential scanning calorimetry and by powder and single crystal x-ray crystallography. In addition, theoretical 13C-NMR chemical shift calculations were also performed for the anhydrous compound and for the first monohydrate, starting from single crystal structures and the structures of these species have now been verified. The first monohydra…

Models MolecularMagnetic Resonance Spectroscopysolid state structure.termoanalyysiPharmaceutical ScienceInfrared spectroscopy13C-CP/MAS-NMR spectroscopy13C-CP/MAS-NMR spektroskopiaFull Research PaperAnalytical ChemistryCrystallcsh:QD241-441Differential scanning calorimetrylcsh:Organic chemistryX-Ray DiffractionDrug Discoverykiinteän tilan rakenneSolid state structurePhysical and Theoretical ChemistrycrystallographyCarbon Isotopeskristallografiathermal Bile acidsCalorimetry Differential ScanningChemistryHydrogen bondOrganic ChemistryTemperatureWaterHydrogen BondingkidetiedeAmidesBile acidsCrystallographysappihapotChemistry (miscellaneous)X-ray crystallographyThermogravimetryAnhydrousCholanesMolecular MedicineOrthorhombic crystal systemSingle crystalthermal analysis
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Evaluation of drug-polymer solubility curves through formal statistical analysis: comparison of preparation techniques.

2014

ABSTRACT: In this study, the influence of the preparation technique (ball milling, spray drying, and film casting) of a supersaturated amorphous dispersion on the quality of solubility determinations of indomethacin in polyvinylpyrrolidone was investigated by means of statistical analysis. After annealing of the amorphous dispersions above the crystallization temperature for 2 h, the solubility curve was derived from the glass transition temperature of the demixed material using the Gordon–Taylor relationship and fitting with the Flory–Huggins model. The study showed that the predicted solubility from the ball-milled mixtures was not consistent with those from spray drying and film casting,…

Models MolecularMaterials scienceHot TemperatureChemistry PharmaceuticalDrug CompoundingIndomethacinAnalytical chemistryPharmaceutical SciencemedicinePharmaceutic AidsSolubilitySupersaturationReproducibilityPolyvinylpyrrolidoneCalorimetry Differential ScanningAnti-Inflammatory Agents Non-SteroidalPovidoneReproducibility of ResultsCastingAmorphous solidChemical engineeringSolubilitySpray dryingEmulsionsGlass transitionPowder Diffractionmedicine.drugJournal of pharmaceutical sciences
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Binding Properties of HABA-Type Azo Derivatives to Avidin and Avidin-Related Protein 4

2006

Summary The chicken genome encodes several biotin-binding proteins, including avidin and avidin-related protein 4 (AVR4). In addition to D -biotin, avidin binds an azo dye compound, 4-hydroxyazobenzene-2-carboxylic acid (HABA), but the HABA-binding properties of AVR4 are not yet known. Differential scanning calorimetry, UV/visible spectroscopy, and molecular modeling were used to analyze the binding of 15 azo molecules to avidin and AVR4. Significant differences are seen in azo compound preferences for the two proteins, emphasizing the importance of the loop between strands β3 and β4 for azo ligand recognition; information on these loops is provided by the high-resolution (1.5 A) X-ray stru…

Models MolecularMolecular modelOvalbuminProtein ConformationClinical BiochemistryCrystallography X-RayLigandsSensitivity and SpecificityBiochemistryAvian Proteinschemistry.chemical_compoundUltraviolet visible spectroscopyBiotinDrug DiscoveryAnimalsMolecular BiologyGlycoproteinschemistry.chemical_classificationPharmacologyAzo compoundBinding SitesbiologyCalorimetry Differential ScanningMolecular StructureStereoisomerismGeneral MedicineLigand (biochemistry)AvidinCombinatorial chemistryCHEMBIOchemistryBiochemistryBiotinylationbiology.proteinMolecular MedicineSpectrophotometry UltravioletGlycoproteinAzo CompoundsChickensAvidinChemistry & Biology
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2NH and 3OH are crucial structural requirements in sphingomyelin for sticholysin II binding and pore formation in bilayer membranes.

2013

AbstractSticholysin II (StnII) is a pore-forming toxin from the sea anemone Stichodactyla heliantus which belongs to the large actinoporin family. The toxin binds to sphingomyelin (SM) containing membranes, and shows high binding specificity for this lipid. In this study, we have examined the role of the hydrogen bonding groups of the SM long-chain base (i.e., the 2NH and the 3OH) for StnII recognition. We prepared methylated SM-analogs which had reduced hydrogen bonding capability from 2NH and 3OH. Both surface plasmon resonance experiments, and isothermal titration calorimetry measurements indicated that StnII failed to bind to bilayers containing methylated SM-analogs, whereas clear bind…

Models MolecularPore Forming Cytotoxic ProteinsMembrane permeabilizationLipid BilayersBiophysicsCalorimetryta3111Biochemistrychemistry.chemical_compoundCnidarian VenomsAnimalsComputer SimulationLipid bilayerta116Binding selectivityUnilamellar LiposomesPhosphocholineBinding SitesMolecular StructureChemistryHydrogen bondVesicleta1182Isothermal titration calorimetryHydrogen BondingCell BiologySurface Plasmon ResonanceProtein Structure TertiarySphingomyelinsKineticsMembraneSea AnemonesBiochemistryMolecular dockingIsothermal titration calorimetryBiophysicsPhosphatidylcholinesSphingomyelinProtein BindingBiochimica et biophysica acta
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Jararhagin-derived RKKH Peptides Induce Structural Changes in α1I Domain of Human Integrin α1β1

2003

Integrin alpha(1)beta(1) is one of four collagen-binding integrins in humans. Collagens bind to the alphaI domain and in the case of alpha(2)I collagen binding is competitively inhibited by peptides containing the RKKH sequence and derived from the metalloproteinase jararhagin of snake venom from Bothrops jararaca. In alpha(2)I, these peptides bind near the metal ion-dependent adhesion site (MIDAS), where a collagen (I)-like peptide is known to bind; magnesium is required for binding. Published structures of the ligand-bound "open" conformation of alpha(2)I differs significantly from the "closed" conformation seen in the structure of apo-alpha(2)I near MIDAS. Here we show that two peptides,…

Models MolecularProtein ConformationStereochemistryIntegrinAlpha (ethology)PeptideCrystallography X-RayBinding CompetitiveBiochemistryCollagen Type IProtein Structure SecondaryIntegrin alpha1beta1Protein structureCrotalid VenomsHumansMagnesiumAmino Acid SequenceBinding siteMolecular BiologyPeptide sequenceFluorescent Dyeschemistry.chemical_classificationBinding SitesCalorimetry Differential ScanningMolecular StructurebiologyMetalloendopeptidasesCell BiologyPeptide FragmentsRecombinant ProteinsSpectrometry FluorescencechemistryJararhaginHelixbiology.proteinCrystallizationJournal of Biological Chemistry
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Irreversible gelation of thermally unfolded proteins:structural and mechanical properties of lysozyme aggregates

2010

The formation of protein aggregates is important in many fields of life science and technology. The morphological and mechanical properties of protein solutions depend upon the molecular conformation and thermodynamic and environmental conditions. Non-native or unfolded proteins may be kinetically trapped into irreversible aggregates and undergo precipitation or gelation. Here, we study the thermal aggregation of lysozyme in neutral solutions. We characterise the irreversible unfolding of lysozyme by differential scanning calorimetry. The structural properties of aggregates and their mechanisms of formation with the eventual gelation are studied at high temperature by spectroscopic, rheolog…

Models MolecularProtein FoldingCircular dichroismGelationProtein ConformationDiffusionBiophysicsProtein aggregationUnfoldingchemistry.chemical_compoundDifferential scanning calorimetryProtein structureAnimalsQuantitative Biology::BiomoleculesChemistryPrecipitation (chemistry)Circular DichroismTemperaturePercolationGeneral MedicineBlood Coagulation FactorsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Thermal irreversibilityCrystallographyChemical physicsThermodynamicsMuramidaseProtein foldingLysozymeProtein aggregation
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Structural and physicochemical characterization of the inclusion complexes of cyclomaltooligosaccharides (cyclodextrins) with melatonin

2002

The stoichiometry, geometry, stability, and solubility of the inclusion complexes of melatonin (MLT) with native cyclomaltooligosaccharides (α-, β- or γ-cyclodextrins, CDs) are determined experimentally by high-resolution NMR spectroscopy, calorimetric and solubility measurements, and mass spectrometry. The observed differences are discussed in terms of molecular recognition expression of the host-guest (h-g) interactions within the hydrophobic CDs cavities of different size. The 1:1 h-g stoichiometry in water solution prevails at low CD concentrations; the trend to form higher order associations is observed at increasing CD concentrations. The stability order β-CD>γ-CD>α-CD for the c…

Models MolecularSpectrometry Mass Electrospray IonizationElectrospray ionizationProtonationCalorimetryCalorimetryMass spectrometryBiochemistryInclusion complexeAnalytical ChemistryExcipientsMolecular recognitionCyclodextrinSolubilityNuclear Magnetic Resonance BiomolecularMelatoninCyclodextrinsMass spectrometryChemistryOrganic ChemistryGeneral MedicineNuclear magnetic resonance spectroscopyNMRCrystallographySolubilityThermodynamicsStoichiometry
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Syntheses and structural study of bile acid amidoalcohols.

2008

Preparation, structural and thermoanalytical characterization of fourteen N-hydroxyalkyl 5beta-cholan-24-amides have been performed in this study. The utilized techniques include liquid state and CP-MAS 13C NMR spectroscopy, thermogravimetry, differential scanning calorimetry, and also powder and single crystal X-ray crystallography. The results were discussed and compared to each other and also to previous findings on similar compounds. One pure hydrate form was obtained. Six new single crystal structures were determined, including one hydrated chloroform solvate. Decomposition temperatures were found to correlate with the side chain length, and the number of the hydroxyl groups. The spati…

Models MolecularSpectrometry Mass Electrospray IonizationMagnetic Resonance SpectroscopyClinical BiochemistryCalorimetryCrystallography X-RayBiochemistryBile Acids and Saltschemistry.chemical_compoundEndocrinologyDifferential scanning calorimetrySide chainMolecular BiologyPharmacologyChloroformCalorimetry Differential ScanningMolecular StructureChemistryOrganic ChemistryNuclear magnetic resonance spectroscopyAmidesThermogravimetryCrystallographyAlcoholsHydrateSingle crystalSteroids
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