Search results for "Carbonic Anhydrase Inhibitors"

showing 10 items of 17 documents

Thermodynamic parameters of the interaction between Co(II) bovine carbonic anhydrase and anionic inhibitors

1992

The pH dependence of the apparent affinity constants of perchlorate for cobalt(II)bovine carbonic anhydrase II has been measured by electronic absorption spectroscopy. The obtained data have been analyzed in terms of the ionization of two acidic groups of CoBCAII, and the affinity of perchlorate for the two water-containing species of the enzyme have been estimated. Furthermore, the affinity constants of nitrate, perchlorate, and azide for CoBCAII in the temperature range 5 degrees C-30 degrees C have been determined by spectrophotometric titrations at pH 7. The affinity constants for these ligands decrease with increasing temperatures. The temperature dependence of binding was used to esti…

AnionsAzidesCarbonic anhydrase IIEnthalpyInorganic chemistrychemistry.chemical_elementBiochemistryInorganic Chemistrychemistry.chemical_compoundPerchlorateCarbonic anhydraseAnimalsPerchloric acidCarbonic Anhydrase InhibitorsCarbonic AnhydrasesNitratesPerchloratesbiologyCobaltKineticschemistrySpectrophotometrybiology.proteinThermodynamicsCattleTitrationAzideCobaltMathematicsJournal of Inorganic Biochemistry
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Induction of carbonic anhydrase in SaOS-2 cells, exposed to bicarbonate and consequences for calcium phosphate crystal formation.

2013

Ca-phosphate/hydroxyapatite crystals constitute the mineralic matrix of vertebrate bones, while Ca-carbonate dominates the inorganic matrix of otoliths. In addition, Ca-carbonate has been identified in lower percentage in apatite crystals. By using the human osteogenic SaOS-2 cells it could be shown that after exposure of the cells to Ca-bicarbonate in vitro, at concentrations between 1 and 10 mm, a significant increase of Ca-deposit formation results. The crystallite nodules formed on the surfaces of SaOS-2 cells become denser and larger in the presence of bicarbonate if simultaneously added together with the mineralization activation cocktail (β-glycerophosphate/ascorbic acid/dexamethason…

Calcium Phosphatesmedicine.drug_classBicarbonateBiophysicschemistry.chemical_elementBioengineering02 engineering and technologyAscorbic AcidCalciumDexamethasoneCell LineBiomaterials03 medical and health scienceschemistry.chemical_compoundCarbonic anhydrasemedicineEscherichia coliHumansCarbonic anhydrase inhibitorBone ResorptionCarbonic Anhydrase InhibitorsSaos-2 cells030304 developmental biologyCarbonic Anhydrases0303 health sciencesbiologyX-RaysGene Expression Regulation Developmental021001 nanoscience & nanotechnologyPhosphateAscorbic acidUp-RegulationAcetazolamideBicarbonatesMicroscopy ElectronchemistryBiochemistryMechanics of MaterialsGlycerophosphatesCeramics and Compositesbiology.protein0210 nano-technologyAcetazolamidemedicine.drugBiomaterials
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X-ray crystallography-promoted drug design of carbonic anhydrase inhibitors.

2015

1-N-Alkylated-6-sulfamoyl saccharin derivatives were prepared and assayed as carbonic anhydrase inhibitors (CAIs). During X-ray crystallographic experiments an unexpected hydrolysis of the isothiazole ring was evidenced which allowed us to prepare highly potent enzyme inhibitors with selectivity for some isoforms with medical applications.

DrugModels MolecularStereochemistryProtein Conformationmedia_common.quotation_subjectCrystallography X-RayCatalysisHydrolysischemistry.chemical_compoundCarbonic anhydraseMaterials ChemistryHumansCarbonic Anhydrase Inhibitorsmedia_commonCarbonic Anhydraseschemistry.chemical_classificationIsothiazolebiologyMetals and AlloysGeneral ChemistryLyaseSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsIsoenzymesEnzymechemistryDrug DesignX-ray crystallographyCeramics and Compositesbiology.proteinSelectivityChemical communications (Cambridge, England)
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Efficient Expression and Crystallization System of Cancer-Associated Carbonic Anhydrase Isoform IX.

2015

Human carbonic anhydrase IX (CA IX) is overexpressed in a number of solid tumors and is considered to be a marker for cellular hypoxia that it is not produced in most normal tissues. CA IX contributes to the acidification of the extracellular matrix, which, in turn, favors tumor growth and metastasis. Therefore, CA IX is considered to be a promising anti-cancer drug target. However, the ability to specifically target CA IX is challenging due to the fact that the human genome encodes 15 different carbonic anhydrase isoforms that have a high degree of homology. Furthermore, structure-based drug design of CA IX inhibitors so far has been largely unsuccessful due to technical difficulties regar…

Gene isoformModels MolecularAntineoplastic AgentsIsozymePichiaPichia pastorisSubstrate SpecificityStructure-Activity RelationshipX-Ray DiffractionAntigens NeoplasmCarbonic anhydraseNeoplasmsDrug DiscoverymedicineStructure–activity relationshipHumansCloning MolecularCarbonic Anhydrase IXCarbonic Anhydrase InhibitorsDatabases ProteinCarbonic Anhydraseschemistry.chemical_classificationbiologyChemistryLyasebiology.organism_classificationAcetazolamideIsoenzymesEnzymeBiochemistrybiology.proteinMolecular MedicineAcetazolamideCrystallizationBaculoviridaemedicine.drugJournal of medicinal chemistry
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5-Substituted-benzylsulfanyl-thiophene-2-sulfonamides with effective carbonic anhydrase inhibitory activity: Solution and crystallographic investigat…

2017

Abstract A series of 5-substituted-benzylsulfanyl-thiophene-2-sulfonamides was prepared by reacting 5-bromo-thiophene-2-sulfonamide with 5-substituted-benzyl mercaptans. The new compounds were investigated as carbonic anhydrase (CA, EC 4.2.1.1) inhibitors. The cytosolic human (h) isoforms hCA I was poorly inhibited by the new sulfonamides (KIs in the range of 683–4250 nM), whereas hCA II, and the transmembrane, tumor associated isoforms hCA IX and XII were effectively inhibited in the subnanomolar–nanomolar range. A high resolution X-ray crystal structure of the adduct of hCA II with one of the new sulfonamides allowed us to rationalize the excellent inhibitory activity of these heterocycli…

Gene isoformModels MolecularStereochemistryClinical BiochemistryPharmaceutical ScienceCrystal structureThiophenesCrystallography X-Ray01 natural sciencesBiochemistryAdductchemistry.chemical_compoundStructure-Activity RelationshipCarbonic anhydraseDrug DiscoveryThiopheneHumansCarbonic Anhydrase InhibitorsMolecular BiologyCarbonic AnhydrasesSulfonamidesbiologyDose-Response Relationship DrugMolecular Structure010405 organic chemistryOrganic ChemistryLyaseTransmembrane protein0104 chemical sciencesSolutions010404 medicinal & biomolecular chemistryCytosolchemistrybiology.proteinMolecular MedicineBioorganicmedicinal chemistry
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N-Substituted and ring opened saccharin derivatives selectively inhibit transmembrane, tumor-associated carbonic anhydrases IX and XII.

2017

A series of N-substituted saccharins incorporating aryl, alkyl and alkynyl moieties, as well as some ring opened derivatives were prepared and investigated as inhibitors of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1). The widespread cytosolic isoforms CA I and II were not inhibited by these sulfonamides whereas transmembrane, tumor-associated ones were effectively inhibited, with KIs in the range of 22.1-481nM for CA IX and of 3.9-245nM for hCA XII. Although the inhibition mechanism of these tertiary/secondary sulfonamides is unknown for the moment, the good efficacy and especially selectivity for the inhibition of the tumor-associated over the cytosolic, widespread isoforms, make…

Gene isoformStereochemistryClinical BiochemistryPharmaceutical Science01 natural sciencesBiochemistrychemistry.chemical_compoundStructure-Activity RelationshipSaccharinAntigens NeoplasmCarbonic anhydraseDrug DiscoveryHumansCarbonic Anhydrase IXCarbonic Anhydrase InhibitorsMolecular BiologyAlkylCarbonic Anhydraseschemistry.chemical_classificationbiologyDose-Response Relationship DrugMolecular Structure010405 organic chemistryArylOrganic ChemistryTransmembrane protein0104 chemical sciences010404 medicinal & biomolecular chemistryCytosolEnzymechemistryBiochemistrybiology.proteinMolecular MedicineSelectivityBioorganicmedicinal chemistry
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3H-1,2-benzoxathiepine 2,2-dioxides: a new class of isoform-selective carbonic anhydrase inhibitors

2017

Abstract A new chemotype with carbonic anhydrase (CA, EC 4.2.1.1) inhibitory action has been discovered, the homo-sulfocoumarins (3H-1,2-benzoxathiepine 2,2-dioxides) which have been designed considering the (sulfo)coumarins as lead molecules. An original synthetic strategy of a panel of such derivatives led to compounds with a unique inhibitory profile and very high selectivity for the inhibition of the tumour associated (CA IX/XII) over the cytosolic (CA I/II) isoforms. Although the CA inhibition mechanism with these new compounds is unknown for the moment, we hypothesize that it may be similar to that of the sulfocoumarins, i.e. hydrolysis to the corresponding sulfonic acids which therea…

Gene isoformStereochemistryHigh selectivityInhibitory postsynaptic potential01 natural sciencesStructure-Activity RelationshipHydrolysisCarbonic anhydraseDrug DiscoveryHumansMoleculeCarbonic Anhydrase InhibitorsCarbonic AnhydrasesPharmacologyCarbonic anhydraseDose-Response Relationship DrugMolecular Structurebiology010405 organic chemistryChemistrylcsh:RM1-950Active sitehomo-sulfocoumarinsGeneral MedicineCyclic S-Oxides0104 chemical sciencesinhibitor010404 medicinal & biomolecular chemistryCytosollcsh:Therapeutics. PharmacologyBiochemistrysulfocoumarinbiology.proteinResearch PaperJournal of Enzyme Inhibition and Medicinal Chemistry
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The efficacy and safety of unfixed and fixed combinations of latanoprost and other antiglaucoma medications.

2002

Adjunctive therapy for the management of glaucoma is commonly used. Unfixed combinations of the prostaglandin analog latanoprost and other glaucoma medications have been demonstrated to effectively lower intraocular pressure (IOP). The range of reported additional reductions in IOP compared to a monotherapy baseline are as follows: latanoprost-timolol (13-37%), latanoprost-pilocarpine 2% (7-14%), latanoprost and carbonic anhydrase inhibitors (15-24.1%), and latanoprost and dipivefrin (15-28%). There is a fixed combination of latanoprost (0.005%) and timolol (0.5%) that has been investigated in Phase III trials in Europe and the United States. In these trials, it was noted that the efficacy …

Intraocular pressureMydriaticsgenetic structuresCombination therapymedicine.medical_treatmentAdrenergic beta-AntagonistsTimololGlaucomachemistry.chemical_compoundMedicineHumansLatanoprostCarbonic Anhydrase InhibitorsAntihypertensive AgentsIntraocular PressureChemotherapyDipivefrinbusiness.industryGlaucomamedicine.diseaseeye diseasesOphthalmologyProstaglandin analogchemistryAnesthesiaProstaglandins F SyntheticLatanoprostDrug Therapy CombinationOcular Hypertensionsense organsOphthalmic SolutionsSafetybusinessmedicine.drugSurvey of ophthalmology
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Update on topical carbonic anhydrase inhibitors

2001

Topical carbonic anhydrase inhibitors are a novel addition to the armamentarium of medical glaucoma treatment; dorzolamide has been available since 1995 and brinzolamide since 1998. They lower intraocular pressure by inhibiting carbonic anhydrase, a key enzyme for aqueous humor formation. Intraocular pressure-lowering activity of the substances appears to be the same and is similar to that of most other agents, but it does not reach the activity of the unselective beta-blocker timolol or the prostaglandin latanoprost. On concomitant treatment, additivity is reached with all other topical agents. A possible improvement of blood flow may offer an additional benefit, but its significance for t…

Intraocular pressuregenetic structuresBrinzolamideThiazinesGlaucomaTimololThiophenesPharmacologyEyeAqueous Humorchemistry.chemical_compoundDorzolamideCarbonic anhydrasemedicineHumansLatanoprostCarbonic Anhydrase InhibitorsAntihypertensive AgentsIntraocular PressureCarbonic Anhydraseschemistry.chemical_classificationSulfonamidesDose-Response Relationship Drugbiologybusiness.industryGlaucomaGeneral Medicinemedicine.diseaseeye diseasesOphthalmologyEnzymechemistryProstaglandins F Syntheticbiology.proteinLatanoprostsense organsOphthalmic SolutionsbusinessBlood Flow Velocitymedicine.drugCurrent Opinion in Ophthalmology
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Interaction of sulphate and chloride with cobalt(II)-carbonic anhydrase

1990

The interaction between Cobalt(II)-Bovine Carbonic Anhydrase II and the inhibitors sulphate and chloride have been investigated through 1H NMR and electronic absorption spectroscopies. Both inhibitors bind to the metal ion forming a 1:1 adduct and the corresponding affinity constants have been determined. These inhibitors interact weakly with CoBCA II and this interaction only occurs at low pH values. The T1 values of the meta-like protons of the coordinated histidines have been measured. The coordination number of the metal ion in the adducts is discussed on the basis of temperature dependence of the isotropic shifts, T1, and molar absorbance values.

Magnetic Resonance SpectroscopyCarbonic anhydrase IICoordination numberInorganic chemistryIon chromatographychemistry.chemical_elementBiochemistryChlorideAdductInorganic ChemistryChloridesCarbonic anhydrasemedicineCarbonic Anhydrase InhibitorsCarbonic AnhydrasesbiologySulfatesChemistryOsmolar ConcentrationTemperatureCobaltHydrogen-Ion ConcentrationSpectrophotometrybiology.proteinProton NMRCobaltmedicine.drugJournal of Inorganic Biochemistry
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