Search results for "hydrophobic"

showing 10 items of 332 documents

Polynucleotide differentiation using hybrid solid-state nanopore functionalizing with α-hemolysin

2019

We report results from full atomistic molecular dynamics simulations on the properties of biomimetic nanopores. This latter result was obtained through the direct insertion of an α-hemolysin protein inside a hydrophobic solid-state nanopore. Upon translocation of different DNA strands, we demonstrate here that the theoretical system presents the same discrimination properties as the experimental one obtained previously. This opens an interesting way to promote the stability of a specific protein inside a solid nanopore to develop further biomimetic applications for DNA or protein sequencing.

Specific proteinPolynucleotidesSolid-state02 engineering and technologyMolecular Dynamics Simulation010402 general chemistry01 natural sciencesHemolysin ProteinsNanoporesMolecular dynamicschemistry.chemical_compoundProtein sequencingBiomimeticsAmino Acid SequenceChemistryHemolysinDNAGeneral Chemistry021001 nanoscience & nanotechnologyCondensed Matter Physics0104 chemical sciencesNanoporePolynucleotideBiophysics0210 nano-technologyHydrophobic and Hydrophilic InteractionsDNASoft Matter
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Profiling of lipid species by normal-phase liquid chromatography, nanoelectrospray ionization, and ion trap–orbitrap mass spectrometry

2013

Detailed analysis of lipid species can be challenging due to their structural diversity and wide concentration range in cells, tissues, and biofluids. To address these analytical challenges, we devised a reproducible, sensitive, and integrated lipidomics workflow based on normal-phase liquid chromatography-Fourier transform mass spectrometry (LC-FTMS) and LC-ITMS(2) (ion trap tandem mass spectrometry) for profiling and structural analysis of lipid species. The workflow uses a normal-phase LC system for efficient separation of apolar and polar lipid species combined with sensitive and specific analysis powered by a chip-based nanoelectrospray ion source and a hybrid ion trap-orbitrap mass sp…

Spectrometry Mass Electrospray IonizationCeramideBiophysicsAnalytical chemistryCeramidesTandem mass spectrometryMass spectrometryOrbitrapBiochemistrylaw.inventionMicechemistry.chemical_compoundTandem Mass Spectrometrylaw3T3-L1 CellsCerebellumIonizationLipidomicsAnimalsMolecular BiologyTriglyceridesChromatographyChemistryCell BiologyIon sourceMice Inbred C57BLIon trapHydrophobic and Hydrophilic InteractionsChromatography LiquidAnalytical Biochemistry
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Molecular mechanism of T-cell protein tyrosine phosphatase (TCPTP) activation by mitoxantrone.

2013

T-cell protein tyrosine phosphatase (TCPTP) is a ubiquitously expressed non-receptor protein tyrosine phosphatase. It is involved in the negative regulation of many cellular signaling pathways. Thus, activation of TCPTP could have important therapeutic applications in diseases such as cancer and inflammation. We have previously shown that the α-cytoplasmic tail of integrin α1β1 directly binds and activates TCPTP. In addition, we have identified in a large-scale high-throughput screen six small molecules that activate TCPTP. These small molecule activators include mitoxantrone and spermidine. In this study, we have investigated the molecular mechanism behind agonist-induced TCPTP activation.…

SpermidineProtein tyrosine phosphataseBiochemistryAnalytical Chemistry0302 clinical medicinePhosphorylationDatabases Protein0303 health sciencesProtein Tyrosine Phosphatase Non-Receptor Type 2biologyChemistrySmall molecule3. Good healthCell biologyisothermal titration calorimetryMolecular Docking Simulationmolecular dynamics simulation030220 oncology & carcinogenesis/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingThermodynamicsHydrophobic and Hydrophilic InteractionsProtein BindingSignal TransductionCell signalingintegrinIntegrinPhosphataseStatic ElectricityBiophysicsAntineoplastic AgentsMolecular Dynamics Simulationta3111mitoxantroneIntegrin alpha1beta1Small Molecule Libraries03 medical and health sciencesSDG 3 - Good Health and Well-beingdifferential scanning fluorimetryHumansBinding siteMolecular Biology030304 developmental biologyT-cell protein tyrosine phosphataseta1182ta3122In vitroProtein Structure TertiaryKineticsCytoplasmbiology.proteinMitoxantronePeptidesBiochimica et Biophysica Acta: Proteins and Proteomics
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Effect of T-R conformational change on sickle-cell hemoglobin interactions and aggregation

2004

We compare the role of a conformational switch and that of a point mutation in the thermodynamic stability of a protein solution and in the consequent propensity toward aggregation. We study sickle-cell hemoglobin (HbS), the beta6 Glu-Val point mutant of adult human hemoglobin (HbA), in its R (CO-liganded) conformation, and compare its aggregation properties to those of both HbS and HbA in their T (unliganded) conformation. Static and dynamic light scattering measurements performed for various hemoglobin concentrations showed critical divergences with mean field exponents as temperature was increased. This allowed determining spinodal data points T(S)(c) by extrapolation. These points were …

SpinodalConformational changeLightProtein ConformationEntropyHemoglobin SickleEnthalpyMolecular ConformationNucleationThermodynamicsProtein aggregationBiochemistryHydrophobic effectDynamic light scatteringStructural BiologySpectroscopy Fourier Transform InfraredHumansPoint MutationScattering RadiationMolecular BiologyCell AggregationCarbon MonoxideChemistryTemperatureProteinsHydrogen-Ion ConcentrationCrystallographyModels ChemicalSpectrophotometryThermodynamicsProtein BindingEntropy (order and disorder)Proteins: Structure, Function, and Bioinformatics
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Low density lipoproteins and human serum albumin as the carriers of squalenoylated drugs: insights from molecular simulations

2018

We have studied the interaction of three clinically promising squalenoylated drugs (gemcitabine-squalene, adenine-squalene, and doxorubicin-squalene) with low-density lipoproteins (LDL) by means of atomistic molecular dynamics simulations. It is shown that all studied squalenoylated drugs accumulate inside the LDL particles. This effect is promoted by the squalene moiety, which acts as an anchor and drives the hydrophilic drugs into the hydrophobic core of the LDL lipid droplet. Our data suggest that LDL particles could be a universal carriers of squalenoylated drugs in the bloodstream. Interaction of gemcitabine-squalene with human serum albumin (HSA) was also studied by ensemble of dockin…

Squalene[PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph]Drug CompoundingPharmaceutical ScienceSerum Albumin Human02 engineering and technologyPlasma protein bindingMolecular Dynamics Simulation010402 general chemistry01 natural sciencesMolecular Docking SimulationDeoxycytidineSqualenechemistry.chemical_compound[ PHYS.PHYS.PHYS-BIO-PH ] Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph]Lipid dropletDrug DiscoverymedicineMoietyHumansComputingMilieux_MISCELLANEOUSDrug CarriersBinding SitesAdenine[SDV.SP]Life Sciences [q-bio]/Pharmaceutical sciences021001 nanoscience & nanotechnologyHuman serum albuminGemcitabine3. Good health0104 chemical sciences[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryLipoproteins LDLMolecular Docking Simulation[ SDV.SP ] Life Sciences [q-bio]/Pharmaceutical scienceschemistryDocking (molecular)Doxorubicin[ CHIM.THEO ] Chemical Sciences/Theoretical and/or physical chemistryBiophysicsMolecular MedicineNanoparticles0210 nano-technologyDrug carrierHydrophobic and Hydrophilic Interactionsmedicine.drugProtein Binding
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Interactions between flavor compounds and food ingredients and their influence on flavor perception

2002

Interactions between flavor compounds and food ingredients are reviewed and their influence on flavor perception is discussed. Proteins are known to bind flavor compounds. For β-lactoglobulin, the most-studied example, hydrophobic interactions with volatiles are described. The effect of the medium on the conformation of the protein and its ability to bind flavor compounds is discussed. In general, the retention of volatiles by protein is much lower than that by fat. In emulsions, however, the presence of protein at the oil/water interface induces a significant effect on flavor release and flavor perception of hydrophobic flavor compounds. For starch, an extensively studied hydrocolloid, amy…

Starch[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process EngineeringGeneral Chemical Engineering01 natural sciencesHydrophobic effectchemistry.chemical_compound0404 agricultural biotechnologyAmylose[SDV.IDA]Life Sciences [q-bio]/Food engineeringFlavor perception[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringFood scienceFlavorAromaComputingMilieux_MISCELLANEOUSbiologyChemistry010401 analytical chemistryfood and beverages04 agricultural and veterinary sciences[SDV.IDA] Life Sciences [q-bio]/Food engineeringequipment and suppliesbiology.organism_classification040401 food science0104 chemical sciencesFood Science
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Binding isotope effects as a tool for distinguishing hydrophobic and hydrophilic binding sites of HIV-1 RT.

2014

The current treatment for HIV-1 infected patients consists of a cocktail of inhibitors, in an attempt to improve the potency of the drugs by adding the possible effects of each supplied compound. In this contribution, nine different inhibitors of HIV-1 RT, one of the three key proteins responsible for the virus replication, have been selected to develop and test a computational protocol that allows getting a deep insight into the inhibitors’ binding mechanism. The interaction between the inhibitors and the protein have been quantified by computing binding free energies through FEP calculations, while a more detailed characterization of the kind of inhibitor–protein interactions is based on …

StereochemistryBinding energyHuman immunodeficiency virus (HIV)Binding energyMolecular Dynamics Simulationmedicine.disease_causeLigandsIsotopesCatalytic DomainKinetic isotope effectDrug DiscoveryMaterials ChemistrymedicinePhysical and Theoretical ChemistryBinding siteBinding isotope effectsIsotopeChemistryWaterHIV Reverse TranscriptaseSurfaces Coatings and FilmsCrystallographyViral replicationHIV-1SolventsQuantum TheoryReverse Transcriptase InhibitorsThermodynamicsFree energiesHydrophobic and Hydrophilic InteractionsProtein BindingThe journal of physical chemistry. B
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The introduction of fluorine atoms or trifluoromethyl groups in short cationic peptides enhances their antimicrobial activity

2006

The effect of introducing fluorine atoms or trifluoromethyl groups in either the peptidic chain or the C-terminal end of cationic pentapeptides is reported. Three series of amide and ester peptides were synthesised and their antimicrobial properties evaluated. An enhanced activity was found in those derivatives whose structure contained fluorine, suggesting an increase in their hydrophobicity.

StereochemistryClinical BiochemistryPharmaceutical Sciencechemistry.chemical_elementPeptideMicrobial Sensitivity TestsBiochemistryChemical synthesisMedicinal chemistryStructure-Activity Relationshipchemistry.chemical_compoundCationsAmideBenzyl CompoundsDrug DiscoveryHumansMolecular Biologychemistry.chemical_classificationTrifluoromethylMolecular StructureOrganic ChemistryCationic polymerizationStereoisomerismBiological activityFluorineAnti-Bacterial AgentsEukaryotic CellschemistryDrug DesignLipophilicityFluorineMolecular MedicineHydrophobic and Hydrophilic InteractionsOligopeptidesBioorganic & Medicinal Chemistry
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Modeling Supramolecular Polymerization: The Role of Steric Effects and Hydrophobic Interactions

2019

We present a combined experimental–simulation study of self-assembly into one-dimensional filaments. Experimentally, we study amphiphilic AuI-metallopeptides in neutral aqueous media. Our model foc...

Steric effectsPolymers and PlasticsAqueous mediumChemistryOrganic ChemistrySupramolecular chemistry02 engineering and technology010402 general chemistry021001 nanoscience & nanotechnology01 natural sciences0104 chemical sciencesInorganic ChemistryHydrophobic effectPolymerizationAmphiphilePolymer chemistryMaterials Chemistry0210 nano-technologyMacromolecules
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Mononuclear rearrangement of heterocycles in zwitterionic micelles of amine oxide surfactants.

2012

Abstract Rate constants for the mononuclear rearrangement (MRH) of Z -phenylhydrazones of some 5-substituted-3-benzoyl-1,2,4-oxadiazoles in water have been measured in the presence of zwitterionic micelles. The use of micellized N -tetradecyl- N , N -dimethylamineoxide (C 14 DMAO) as the reaction medium allowed to solubilize the otherwise water-insoluble oxadiazoles. Micellar rate effects were analyzed by using a simple pseudo-phase model and compared with those obtained in non-ionic micelles (Triton X-100). Evidence that both the rate of the rearrangement reaction and the binding of the substrates to the micelles are mainly governed by substrate hydrophobicity is obtained. The disagreement…

Steric effectsSpectrometry Mass Electrospray IonizationN-tetradecyl-NOctoxynolPhotochemistryMicelleMononuclear rearrangements of heterocycles (MHRs)Biomaterialschemistry.chemical_compoundSurface-Active AgentsColloid and Surface ChemistryReaction rate constantMicellar catalysiN-tetradecyl-NN-dimethylamineoxidePolymer chemistryRearrangement reactionzwitterionic micelleMicellesOxadiazolesHydrazonesSubstrate (chemistry)WaterSettore CHIM/06 - Chimica OrganicaSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsAmine oxideKineticschemistrySolubilitySolubilizationN-dimethylamineoxideThermodynamicsHydrophobic and Hydrophilic InteractionsMyristic AcidsDimethylaminesJournal of colloid and interface science
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