Search results for "conformation"

showing 10 items of 1414 documents

Cation binding resorcinarene bis-crowns: the effect of lower rim alkyl chain length on crystal packing and solid lipid nanoparticles

2012

A group of seven resorcinarene bis-crown ethers (CNBC5) with two polyether bridges at the upper rim and either propyl, butyl, pentyl, heptyl, nonyl, decyl or undecyl groups at the lower rim were synthesized and their binding properties with Cs+ were investigated by NMR titration. The bis-crowns form 1:2 complexes with Cs+ with binding constants of logK 4–5. Crystal structures of bis-crowns and their Cs+ and K+ complexes were studied and different packing motifs were found depending on the alkyl chain length. Short ethyl, propyl and butyl alkyl chains gave a layer or pillar packing where the polar and non-polar regions cannot be distinguished, whereas longer pentyl and decyl chains formed bi…

Cation bindingkaliumStereochemistryydinmagneettinen resonanssiCyclohexane conformationsolid lipid nanoparticleamphiphileCrystal structureCatalysisCrystalcesiumAmphiphilesupramolekyylikemiaMaterials Chemistrykiinteä lipidipartikkelisupramolekulaarinen kemiaMoleculemacrocyclic compoundta116Alkylkaliksareeniitsejärjestäytyminenchemistry.chemical_classificationresorcinareneChemistryGeneral Chemistrycaesiumself-assemblyResorcinarenekompleksiCrystallographynuclear magnetic resonanceamfifiilimakrosyklinen yhdistecalixarenecomplexröntgenkristallografiaresorsinareeni
researchProduct

Streptolysin O: the C-terminal, tryptophan-rich domain carries functional sites for both membrane binding and self-interaction but not for stable oli…

2001

AbstractStreptolysin O belongs to the class of thiol-activated toxins, which are single chain, four-domain proteins that bind to membranes containing cholesterol and then assemble to form large oligomeric pores. Membrane binding involves a conserved tryptophan-rich sequence motif located within the C-terminally located domain 4. In contrast, sites involved in oligomerization and pore formation have been assigned to domains 1 and 3, respectively. We here examined the functional properties of domain 4, which was recombinantly expressed with an N-terminal histidine tag for purification and an additional cysteine residue for covalent labeling. The fluorescently labeled fragment readily bound to…

Cell Membrane PermeabilityMembrane bindingProtein ConformationBiophysicsPlasma protein bindingBiochemistryThiol-activated toxinStructure-Activity RelationshipProtein structureBacterial ProteinsProtein oligomerizationHumansProtein oligomerizationBinding sitePore-forming toxinBinding SitesChemistryErythrocyte MembraneCell BiologyMembraneBiochemistryMutationStreptolysinsBiophysicsPore-forming toxinFluoresceinStreptolysinSequence motifProtein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
researchProduct

Assembly mechanism of the oligomeric streptolysin O pore: the early membrane lesion is lined by a free edge of the lipid membrane and is extended gra…

1998

Streptolysin O (SLO) is a bacterial exotoxin that binds to cell membranes containing cholesterol and then oligomerizes to form large pores. Along with rings, arc-shaped oligomers form on membranes. It has been suggested that each arc represents an incompletely assembled oligomer and constitutes a functional pore, faced on the opposite side by a free edge of the lipid membrane. We sought functional evidence in support of this idea by using an oligomerization-deficient, non-lytic mutant of SLO. This protein, which was created by chemical modification of a single mutant cysteine (T250C) with N-(iodoacetaminoethyl)-1-naphthylamine-5-sulfonic acid, formed hybrid oligomers with active SLO on memb…

Cell Membrane PermeabilityProtein ConformationMembrane lipidsBiologyCholesterol-dependent cytolysinComplement Hemolytic Activity AssayOligomerGeneral Biochemistry Genetics and Molecular BiologyMembrane Lipidschemistry.chemical_compoundBacterial ProteinsNaphthalenesulfonatesAnimalsProtein oligomerizationCysteineLipid bilayerMolecular BiologyGeneral Immunology and MicrobiologyGeneral NeuroscienceErythrocyte MembraneCalceinMembranechemistryBiochemistryMutationStreptolysinsBiophysicsStreptolysinRabbitsResearch ArticleThe EMBO Journal
researchProduct

A specific CD4 epitope bound by tregalizumab mediates activation of regulatory T cells by a unique signaling pathway

2014

CD4(+)CD25(+) regulatory T cells (Tregs) represent a specialized subpopulation of T cells, which are essential for maintaining peripheral tolerance and preventing autoimmunity. The immunomodulatory effects of Tregs depend on their activation status. Here we show that, in contrast to conventional anti-CD4 monoclonal antibodies (mAbs), the humanized CD4-specific monoclonal antibody tregalizumab (BT-061) is able to selectively activate the suppressive properties of Tregs in vitro. BT-061 activates Tregs by binding to CD4 and activation of signaling downstream pathways. The specific functionality of BT-061 may be explained by the recognition of a unique, conformational epitope on domain 2 of th…

Cell signalingProtein Conformationmedicine.drug_classMolecular Sequence DataImmunologyAntibodies Monoclonal HumanizedCrystallography X-RayLymphocyte ActivationMonoclonal antibodyT-Lymphocytes RegulatoryEpitopeT-Lymphocyte SubsetsTransforming Growth Factor betamedicineHumansImmunology and Allergyddc:610Amino Acid SequenceIL-2 receptorPhosphorylationCells CulturedbiologyInterleukin-2 Receptor alpha SubunitAntibodies MonoclonalPeripheral toleranceCell BiologyTransforming growth factor betaMolecular biologyCell biologyCD4 Antigensbiology.proteinEpitopes B-LymphocyteSignal transductionImmunosuppressive AgentsProtein BindingSignal TransductionConformational epitopeImmunology & Cell Biology
researchProduct

Improved synthesis and in vitro evaluation of the cytotoxic profile of oxysterols oxidized at C4 (4α- and 4β-hydroxycholesterol) and C7 (7-ketocholes…

2013

Whereas the biological activities of oxysterols oxidized at C7 (7-ketocholesterol (7KC), 7β-hydroxycholesterol (7β-OHC), 7α-hydroxycholesterol (7α-OHC)) are well documented, those of oxysterols oxidized at C4 (4β-hydroxycholesterol (4β-OHC), 4α-hydroxycholesterol (4α-OHC)) are not well known, especially on the cells of the central nervous system. Therefore, an improved methodology has been validated for 4β-OHC and 4α-OHC synthesis, and the effects on cell viability and cell growth of these molecules were studied on immortalized, tumoral and normal brain cells (158N, C6 and SK-N-BE cells, and mixed primary cultures of astrocytes and oligodendrocytes). Whereas inhibition of cell growth with 7…

Central Nervous SystemCell SurvivalCentral nervous systemMolecular ConformationCell LineStructure-Activity RelationshipDrug Discoverypolycyclic compoundsmedicineHumansCytotoxic T cellViability assayKetocholesterolsCell ProliferationPharmacologyDose-Response Relationship DrugChemistryCell growthOrganic ChemistryGeneral MedicineHydroxycholesterolsIn vitroSterolsOn cellsmedicine.anatomical_structureBiochemistryToxicitylipids (amino acids peptides and proteins)sense organs4β hydroxycholesterolOxidation-ReductionEuropean Journal of Medicinal Chemistry
researchProduct

Oligomerization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target memb…

1999

Vibrio cholerae cytolysin permeabilizes animal cell membranes. Upon binding to the target lipid bilayer, the protein assembles into homo-oligomeric pores of an as yet unknown stoichiometry. Pore formation has been observed with model liposomes consisting of phosphatidylcholine and cholesterol, but the latter were much less susceptible to the cytolysin than were erythrocytes or intestinal epithelial cells. We here show that liposome permeabilization is strongly promoted if cholesterol is combined with sphingolipids, whereby the most pronounced effects are observed with monohexosylceramides and free ceramide. These two lipid species are prevalent in mammalian intestinal brush border membranes…

CeramideCell Membrane PermeabilityPentamerProtein ConformationGalactosylceramidesBiologymedicine.disease_causeBiochemistrychemistry.chemical_compoundPhosphatidylcholinemedicineHumansLipid bilayerMolecular BiologyVibrio choleraeCells CulturedLiposomeSphingolipidsCytotoxinsBrainCell BiologyFluoresceinsLipid MetabolismMembraneCholesterolBiochemistrychemistryVibrio choleraeLiposomesElectrophoresis Polyacrylamide GelCytolysinIsoelectric FocusingThe Journal of biological chemistry
researchProduct

Comparative computational analysis of different active site conformations and substrates in a chalcone isomerase catalyzed reaction.

2006

Chalcone isomerase catalyzes the transformation of chalcones to flavanones. We present a computational study of the rate-limiting chemical step, an intramolecular Michael addition of a 2'-oxyanion to the alpha,beta-double bound. By using quantum mechanical/molecular mechanical hybrid methods we traced the free-energy profiles associated with the reaction of two different substrates (chalcone and 6'-deoxychalcone) in two different conformations of the active site that are described in the different crystallographic structures available. We have obtained significant differences (about 4 kcal/mol) in the free-energy barriers calculated for the two active sites. According to our results, the ac…

Chalcone isomeraseAnionsModels MolecularChalconeStereochemistryProtein ConformationMolecular ConformationCatalysisCatalysischemistry.chemical_compoundAtomMaterials ChemistryComputer SimulationPhysical and Theoretical ChemistryIntramolecular LyasesBinding SitesbiologyActive siteSubstrate (chemistry)Hydrogen-Ion ConcentrationCarbonSurfaces Coatings and FilmsKineticschemistryModels ChemicalIntramolecular forcebiology.proteinMichael reactionQuantum TheoryThermodynamicsSoftwareThe journal of physical chemistry. B
researchProduct

Enzymatic effects on reactant and transition states. The case of chalcone isomerase.

2007

Chalcone isomerase catalyzes the transformation of chalcone to naringerin as a part of flavonoid biosynthetic pathways. The global reaction takes place through a conformational change of the substrate followed by chemical reaction, being thus an excellent example to analyze current theories about enzyme catalysis. We here present a detailed theoretical study of the enzymatic action on the conformational pre-equilibria and on the chemical steps for two different substrates of this enzyme. Free-energy profiles are obtained in terms of potentials of mean force using hybrid quantum mechanics/molecular mechanics potentials. The role of the enzyme becomes clear when compared to the counterpart eq…

Chalcone isomeraseChalconeStereochemistryProtein ConformationCrystallography X-RayBiochemistryChemical reactionCatalysisEnzyme catalysischemistry.chemical_compoundColloid and Surface ChemistryChalconeChalconesComputational chemistryTransition state analogIntramolecular LyasesBinding SitesbiologyChemistrySubstrate (chemistry)Active siteStereoisomerismGeneral ChemistryTransition stateKineticsbiology.proteinJournal of the American Chemical Society
researchProduct

A Rational Design for Imidazolate-Bridged Linear Trinuclear Compounds from Mononuclear Copper(II) Complexes with 2-[((Imidazol-2-ylmethylidene)amino)…

2001

Two mononuclear copper(II) complexes with the unsymmetrical tridentate ligand 2-[((imidazol-2-ylmethylidene)amino)ethyl]pyridine (HL), [Cu(HL)(H2O)](ClO4)2.2H2O (1) and [Cu(HL)Cl2] (2), have been prepared and characterized. The X-ray analysis of 2 revealed that the copper(II) ion assumes a pentacoordinated square pyramidal geometry with an N3Cl2 donor set. When 1 and 2 are treated with an equimolecular amount of potassium hydroxide, the deprotonation of the imidazole moiety promotes a self-assembled process, by coordination of the imidazolate nitrogen atom to a Cu(II) center of an adjacent unit, leading to the polynuclear complexes [[Cu(L)(H2O)](ClO4)]n (3) and [[Cu(L)Cl].2H2O]n (4). Variab…

Chemical PhenomenaPyridinesStereochemistryMolecular Conformationchemistry.chemical_elementCrystallography X-RayLigandsInorganic ChemistryMagneticschemistry.chemical_compoundDeprotonationImidazolatePyridineOrganometallic CompoundsImidazolePhysical and Theoretical ChemistryIsostructuralChemistry PhysicalChemistryLigandImidazolesHydrogen BondingCopperSquare pyramidal molecular geometryCrystallographyCopperInorganic Chemistry
researchProduct

Sharp and fast: sensors and switches based on polymer brushes with adsorption-active minority chains.

2014

We propose a design for polymer-based sensors and switches with sharp switching transition and fast response time. The switching mechanism involves a radical change in the conformations of adsorption-active minority chains in a brush. Such transitions can be induced by a temperature change of only about ten degrees, and the characteristic time of the conformational change is less than a second. We present an analytical theory for these switches and support it by self-consistent field calculations and Brownian dynamics simulations.

Chemical Physics (physics.chem-ph)chemistry.chemical_classificationMaterials sciencePolymersMolecular ConformationFOS: Physical sciencesGeneral Physics and AstronomyNanotechnologyAdhesionPolymerCondensed Matter - Soft Condensed MatterKineticsAdsorptionchemistryChemical engineeringModels ChemicalPhysics - Chemical PhysicsPolymer coatingSoft Condensed Matter (cond-mat.soft)ThermodynamicsPhysical review letters
researchProduct