Search results for "Protein Binding"

showing 10 items of 870 documents

Structural analysis of copper(I) interaction with amyloid β peptide

2019

Abstract The N-terminal fragment of Aβ (β = beta) peptide is able to bind essential transition metal ions like, copper, zinc and iron. Metal binding usually occurs via the imidazole nitrogens of the three His residues which play a key role in the coordination chemistry. Among all the investigated systems, the interaction between copper and Amyloid β assume a biological relevance because of the interplay between the two copper oxidation states, Cu(II) and Cu(I), and their involvement in redox reactions. Both copper ions share the ability to bind Amyloid β. A huge number of investigations have demonstrated that Cu(II) anchors to the N-terminal amino and His6, His13/14 imidazole groups, while …

AmyloidSilverCoordination spherechemistry.chemical_elementPeptide010402 general chemistrySilver(I)01 natural sciencesBiochemistryRedoxCoordination complexInorganic ChemistryMetalchemistry.chemical_compoundCoordination ComplexesImidazoleHistidineAmino Acid SequenceHistidinechemistry.chemical_classificationAmyloid beta-Peptides010405 organic chemistryChemistryStructureCopperPeptide Fragments0104 chemical sciencesCrystallographyCoordinationvisual_artvisual_art.visual_art_mediumCopper(I)CopperProtein BindingJournal of Inorganic Biochemistry
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Factors influencing the interaction of herpes simplex virus glycoprotein C with the third component of complement.

1992

The factors influencing the interaction of herpes simplex virus (HSV) glycoprotein C (gC) with the third component of complement (C3) were investigated in this study. The ability of gC of HSV type 1 (gC-1) to bind to the C3b fragment of C3 was found to be influenced by cell specific processing of gC-1 in a different manner, binding being remarkably enhanced in some cell lines following removal of sialic acid residues. Testing several intertypic recombinants of HSV we found that only strains expressing gC-1 exhibited binding to C3b, even though their genome consisted mainly of HSV-2 sequences in some recombinants. Expression of type-2 glycoproteins gB, gD, gE, gG, gH, and gI did not alter th…

AnionsRosette FormationMolecular Sequence DataBiologyIn Vitro Techniquesmedicine.disease_causeViruschemistry.chemical_compoundStructure-Activity RelationshipViral Envelope ProteinsVirologymedicineTumor Cells CulturedAnimalsHumansSimplexvirusAmino Acid SequenceVero Cellschemistry.chemical_classificationHeparinTemperatureGeneral MedicineNeomycinHerpesvirus glycoprotein BVirologySialic acidHerpes simplex viruschemistryComplement C3bVero cellbiology.proteinAntibodyGlycoproteinmedicine.drugProtein BindingArchives of virology
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Comparative analysis of the electrostatics of the binding of cationic proteins to vesicles: Asymmetric location of anionic phospholipids

2009

The role of electrostatics is studied in the adsorption of cationic proteins to zwitterionic phosphatidylcholine (PC) and anionic PC/phosphatidylglycerol (PG) mixed small unilamellarvesicles (SUVs). For model proteins the interaction is monitored vs. PG content at low ionic strength. The adsorption of lysozyme and myoglobin (isoelectric point, pl 7-11) is investigated in SUVs, along with changes of the fluorescence emission spectra of the cationic proteins, via their adsorption on SUVs. In the Gouy-Chapman formalism, the activity coefficient goes with the square of charge number. Deviations from the ideal model could indicate the asymmetric location of the anionic phospholipid in the bilaye…

AnionsStatic ElectricityFluorescence spectrometryAnalytical chemistryBiochemistryAnalytical Chemistrychemistry.chemical_compoundCationsEnvironmental ChemistryProtein–lipid interactionPhospholipidsUnilamellar LiposomesSpectroscopyMyoglobinChemistryBilayerOsmolar ConcentrationCationic polymerizationProteinsCharge numberPhosphatidylglycerolsCrystallographySpectrometry FluorescenceIsoelectric pointMyoglobinIonic strengthPhosphatidylcholinesMuramidaseProtein BindingAnalytica Chimica Acta
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A Novel Series of Acylhydrazones as Potential Anti-Candida Agents: Design, Synthesis, Biological Evaluation and In Silico Studies

2019

In the context of an increased incidence of invasive fungal diseases, there is an imperative need of new antifungal drugs with improved activity and safety profiles. A novel series of acylhydrazones bearing a 1,4-phenylene-bisthiazole scaffold was designed based on an analysis of structures known to possess anti-Candida activity obtained from a literature review. Nine final compounds were synthesized and evaluated in vitro for their inhibitory activity against various strains of Candida spp. The anti-Candida activity assay revealed that some of the new compounds are as active as fluconazole against most of the tested strains. A molecular docking study was conducted in order to evaluate the …

Antifungal AgentsMolecular modelIn silicoPharmaceutical ScienceContext (language use)anti-CandidaMicrobial Sensitivity Tests01 natural sciencesArticleAnalytical Chemistrylcsh:QD241-44103 medical and health scienceschemistry.chemical_compoundStructure-Activity Relationshiplcsh:Organic chemistryDrug DiscoverymedicinePhysical and Theoretical ChemistryFluconazole030304 developmental biologyCandida0303 health sciencesMolecular Structure010405 organic chemistrymolecular modelingLanosterolOrganic Chemistryanti-<i>Candida</i>HydrazonesBiological activityIn vitro0104 chemical sciencesMolecular Docking Simulationlanosterol 14α-demethylaseADMETchemistryBiochemistryDesign synthesisChemistry (miscellaneous)Drug DesignMolecular MedicinethiazoleFluconazoleacylhydrazonemedicine.drugProtein BindingMolecules
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Ag+ Complexes as Potential Therapeutic Agents in Medicine and Pharmacy

2019

Silver is a non-essential element with promising antimicrobial and anticancer properties. This work is a detailed summary of the newest findings on the bioinorganic chemistry of silver, with a special focus on the applications of Ag+ complexes and nanoparticles. The coordination chemistry of silver is given a reasonable amount of attention, summarizing the most common silver binding sites and giving examples of such binding motifs in biologically important proteins. Possible applications of this metal and its complexes in medicine, particularly as antibacterial and antifungal agents and in cancer therapy, are discussed in detail. The most recent data on silver nanoparticles are also summari…

Antifungalsilver nanoparticlesSilvermedicine.drug_classCancer therapyMetal NanoparticlesNanoparticleAntineoplastic Agents02 engineering and technologyPharmacology010402 general chemistry01 natural sciencesBiochemistrySilver(I) complexesSilver nanoparticleCoordination complexStructure-Activity RelationshipAnti-Infective AgentsCoordination ComplexesDrug DiscoverymedicineHumansAmino Acid SequenceAmino AcidsIonsPharmacologychemistry.chemical_classificationMolecular StructureChemistryOrganic Chemistryantibacterial and anticancer activity of Ag+021001 nanoscience & nanotechnologyCombinatorial chemistry0104 chemical sciencescysteine and methionine motifsMolecular Medicine0210 nano-technologyProtein BindingCurrent Medicinal Chemistry
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Interaction of theEscherichia colitransporter DctA with the sensor kinase DcuS: presence of functional DctA/DcuS sensor units

2012

The aerobic Escherichia coli C(4) -dicarboxylate transporter DctA and the anaerobic fumarate/succinate antiporter DcuB function as obligate co-sensors of the fumarate responsive sensor kinase DcuS under aerobic or anaerobic conditions respectively. Overproduction under anaerobic conditions allowed DctA to replace DcuB in co-sensing, indicating their functional equivalence in this capacity. In vivo interaction studies between DctA and DcuS using FRET or a bacterial two-hybrid system (BACTH) demonstrated their interaction. DctA-YFP bound to an affinity column and was able to retain DcuS. DctA shows substantial sequence and secondary structure conservation to Glt(Ph), the Na(+)/glutamate sympo…

AntiporterPlasma protein bindingBiologybiology.organism_classificationmedicine.disease_causeMicrobiologyPyrococcus horikoshiiTransmembrane domainBiochemistryHelixSymportermedicineMolecular BiologyEscherichia coliProtein secondary structureMolecular Microbiology
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Sulphoevernan, a polyanionic polysaccharide, and the narcissus lectin potently inhibit human immunodeficiency virus infection by binding to viral env…

1990

Sulphoevernan is a sulphated alpha-1----3, 1----4 polyglucan (Mr 20,000) with a helical structure. This compound effectively inhibits both human immunodeficiency virus type 1 (HIV-1) and type 2 infection of cells in vitro at concentrations around 0.5 micrograms/ml. Moreover, the compound completely inhibits HIV-1-induced syncytium formation at a concentration of 1 microgram/ml. Competition experiments with 35S-labelled sulphoevernan revealed that the mannose-specific lectin from Narcissus pseudonarcissus prevented binding of sulphoevernan to HIV-1, whereas the antibody OKT4A did not reduce the amount of sulphoevernan bound to MT-2 cells. These data indicate that the non-cytotoxic polymer su…

Antiviral AgentsVirusCell LineViral envelopeViral Envelope ProteinsIn vivoPolysaccharidesVirologyLectinsMurine leukemia virusHumansGlucansSyncytiumbiologyLectinbiology.organism_classificationVirologyIn vitroHIV-2biology.proteinHIV-1AntibodyPlant LectinsZidovudineCell DivisionProtein BindingThe Journal of general virology
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Azapropazone binding to human serum albumin

1980

Azapropazone, a new non-steroidal antiinflammatory drug, is strongly bound to human serum albumin. As revealed by Scatchard analysis, one high-affinity binding site with an association constant of about 1.2 x 10(6)M-1 and two low-affinity binding sites with association constants of about 0.05 x 10(6)M-1 were found. While the high-affinity binding site of azapropazone is clearly not identical with the diazepam or digitoxin binding sites of human serum albumin, contradictory evidence was found by optical measurements and displacement studies for the similarity of the azapropazone and the warfarin binding site of human serum albumin. At present, it is suggested that both drugs bind to differen…

ApazoneDigitoxinOptical measurementsEndogenyPlasma protein bindingIn Vitro TechniquesPharmacologyBinding CompetitivemedicineHumansBinding siteSerum AlbuminAzapropazonePharmacologyBinding SitesAntiinflammatory drugTriazinesChemistryCircular DichroismGeneral MedicineHuman serum albuminPhenylbutazoneBiochemistryDialysisProtein Bindingmedicine.drugNaunyn-Schmiedeberg's Archives of Pharmacology
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Uptake mechanism of ApoE-modified nanoparticles on brain capillary endothelial cells as a blood-brain barrier model.

2012

Background The blood-brain barrier (BBB) represents an insurmountable obstacle for most drugs thus obstructing an effective treatment of many brain diseases. One solution for overcoming this barrier is a transport by binding of these drugs to surface-modified nanoparticles. Especially apolipoprotein E (ApoE) appears to play a major role in the nanoparticle-mediated drug transport across the BBB. However, at present the underlying mechanism is incompletely understood. Methodology/Principal Findings In this study, the uptake of the ApoE-modified nanoparticles into the brain capillary endothelial cells was investigated to differentiate between active and passive uptake mechanism by flow cytome…

Apolipoprotein EDrugs and DevicesDrug Research and DevelopmentLipoproteinsMaterials Sciencelcsh:MedicinePlasma protein bindingBiologyBlood–brain barrierBiochemistryFlow cytometryApolipoproteins EMaterial by AttributeMiceApolipoproteins EDrug Delivery Systemsddc:570Cell Line TumormedicineAnimalsHumansNanotechnologyPharmacokineticsReceptorlcsh:ScienceBiologySerum AlbuminBrain DiseasesMultidisciplinaryMicroscopy Confocalmedicine.diagnostic_testlcsh:RBrainEndothelial CellsProteinsBiological TransportFlow CytometryCell biologymedicine.anatomical_structureBlood-Brain BarrierNanoparticles for drug delivery to the brainLDL receptorNanoparticlesMedicinelcsh:QProtein BindingResearch ArticleBiotechnologyPLoS ONE
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Haptoglobin interacts with apolipoprotein E and beta-amyloid and influences their crosstalk.

2014

Beta-amyloid accumulation in brain is a driving force for Alzheimer's disease pathogenesis. Apolipoprotein E (ApoE) represents a critical player in beta-amyloid homeostasis, but its role in disease progression is controversial. We previously reported that the acute-phase protein haptoglobin binds ApoE and impairs its function in cholesterol homeostasis. The major aims of this study were to characterize the binding of haptoglobin to beta-amyloid, and to evaluate whether haptoglobin affects ApoE binding to beta-amyloid. Haptoglobin is here reported to form a complex with beta-amyloid as shown by immunoblotting experiments with purified proteins, or by its immunoprecipitation in brain tissues …

Apolipoprotein EMalePhysiologyDiseaseBeta-amyloidBiochemistryAmyloid beta-Protein PrecursorAlzheimer' diseasepolycyclic compoundsskin and connective tissue diseasesapolipoprotein EbiologyChemistryMedicine (all)Haptoglobinfood and beveragesBrainApoE/A? complexGeneral MedicineMiddle AgedhaptoglobinCrosstalk (biology)ApoE/Aβ complexSettore MED/26 - Neurologialipids (amino acids peptides and proteins)FemaleAlzheimer's diseaseProtein BindingAdultmedicine.medical_specialtyImmunoprecipitationCognitive NeuroscienceEnzyme-Linked Immunosorbent AssayCHO CellsTransfectionAlzheimer' disease; ApoE/Aβ complex; Apolipoprotein E; Beta-amyloid; Haptoglobin; Human brain tissue; Adult; Aged; Alzheimer Disease; Amyloid beta-Peptides; Amyloid beta-Protein Precursor; Analysis of Variance; Animals; Apolipoproteins E; Brain; CHO Cells; Cricetulus; Enzyme-Linked Immunosorbent Assay; Female; Haptoglobins; Humans; Immunoprecipitation; Male; Middle Aged; Mutation; Protein Binding; Transfection; Biochemistry; Cell Biology; Physiology; Cognitive Neuroscience; Medicine (all)NOApolipoproteins ECricetulusAlzheimer DiseaseInternal medicinemental disordersmedicineAnimalsHumansImmunoprecipitationAgedAnalysis of VarianceAmyloid beta-PeptidesHaptoglobinsNeurotoxicityAlzheimer’diseaseCell Biologymedicine.diseasehuman brain tissueEndocrinologyMutationbiology.proteinAlzheimer'diseaseHomeostasisACS chemical neuroscience
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