Search results for " cross-linking"

showing 10 items of 11 documents

Production of Injectable Marine Collagen-Based Hydrogel for the Maintenance of Differentiated Chondrocytes in Tissue Engineering Applications

2020

Cartilage is an avascular tissue with limited ability of self-repair. The use of autologous chondrocyte transplants represent an effective strategy for cell regeneration

0301 basic medicineAquatic OrganismsScyphozoaCytoskeleton organizationchondrocytes02 engineering and technologychondrocytes differentiationGelatinRegenerative medicinelcsh:ChemistryMiceTissue engineeringcartilagelcsh:QH301-705.5CytoskeletonSpectroscopyGlycosaminoglycansChemistryCell DifferentiationHydrogelsdifferentiationGeneral Medicine021001 nanoscience & nanotechnologyComputer Science ApplicationsCell biologymedicine.anatomical_structurejellyfish collagenenzymatic cross-linkingchondrocyteCollagen0210 nano-technologyfood.ingredientCell Survivalregenerative medicineArticleCatalysisChondrocyteCell LineInjectionsInorganic Chemistry03 medical and health sciencesfoodmedicineAnimalsPhysical and Theoretical ChemistryMolecular BiologyTissue EngineeringRegeneration (biology)CartilageOrganic ChemistryChondrogenesisRats030104 developmental biologyGene Expression Regulationlcsh:Biology (General)lcsh:QD1-999gene expressionCattlecomposite injectable hydrogelInternational Journal of Molecular Sciences
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Human Achilles tendon glycation and function in diabetes

2016

Diabetic patients have an increased risk of foot ulcers, and glycation of collagen may increase tissue stiffness. We hypothesized that the level of glycemic control (glycation) may affect Achilles tendon stiffness, which can influence gait pattern. We therefore investigated the relationship between collagen glycation, Achilles tendon stiffness parameters, and plantar pressure in poorly ( n = 22) and well ( n = 22) controlled diabetic patients, including healthy age-matched (45–70 yr) controls ( n = 11). There were no differences in any of the outcome parameters (collagen cross-linking or tendon stiffness) between patients with well-controlled and poorly controlled diabetes. The overall effe…

0301 basic medicineBlood GlucoseMaleGlycosylationPhysiologyFoot/physiologyDiabetes Mellitus/physiopathologychemistry.chemical_compound0302 clinical medicineGlycationta315GaitAchilles tendondiabetesBiomechanical Phenomena/physiologyta3141ta3142Middle Agedenzymatic and non-enzymatic collagen cross-linkingAchilles Tendon/physiopathologymusculoskeletal systemTendonBiomechanical Phenomenamedicine.anatomical_structureGait/physiologymusculoskeletal diseasesmedicine.medical_specialtyUrologyConnective tissue030209 endocrinology & metabolismta3111Achilles TendonGlycemic Index/physiology03 medical and health sciencesPhysiology (medical)Diabetes mellitusJoint capsulemedicineDiabetes MellitusHumansPentosidinebusiness.industryFootForefootmedicine.diseasefoot ulcerSurgerybody regionsBlood Glucose/physiology030104 developmental biologyCross-Sectional StudieschemistryGlycemic IndexAchilles tendon mechanicsEnzymatic and nonenzymatic collagen cross-linkingbusiness
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Transmembrane signaling and cytoplasmic signal conversion by dimeric transmembrane helix 2 and a linker domain of the DcuS sensor kinase

2020

Transmembrane (TM) signaling is a key process of membrane-bound sensor kinases. The C4-dicarboxylate (fumarate) responsive sensor kinase DcuS of Escherichia coli is anchored by TM helices TM1 and TM2 in the membrane. Signal transmission across the membrane relies on the piston-type movement of the periplasmic part of TM2. To define the role of TM2 in TM signaling, we use oxidative Cys cross-linking to demonstrate that TM2 extends over the full distance of the membrane and forms a stable TM homodimer in both the inactive and fumarate-activated state of DcuS. An S186xxxGxxxG194 motif is required for the stability and function of the TM2 homodimer. The TM2 helix further extends on the periplas…

0301 basic medicineCytoplasmGpA glycophorin AC4DC C4-dicarboxylateCL cross-linkingpiston-typeMBP maltose-binding proteinBiochemistry03 medical and health sciencesProtein DomainsDcuSEscherichia coli(Gly)xxx(Gly) motifMolecular Biologysensor kinasefumarate030102 biochemistry & molecular biologyChemistryEscherichia coli ProteinsCell MembraneHistidine kinaseGene Expression Regulation BacterialCell BiologyPeriplasmic spacelinkerTransmembrane proteinoxidative Cys cross-linkingTransmembrane domain030104 developmental biologyMembrane proteinProtein kinase domainHelixBiophysicsProtein MultimerizationProtein Kinasestransmembrane signalingLinkerResearch ArticleTM transmembraneJournal of Biological Chemistry
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The Low-Affinity ATP Binding Site of the Escherichia coli SecA Dimer Is Localized at the Subunit Interface

1997

The homodimeric SecA protein is the ATP-dependent force generator in the Escherichia coli precursor protein translocation cascade. SecA contains two essential nucleotide binding sites (NBSs), i.e., NBS1 and NBS2 that hind ATP with high and low affinity, respectively. The photoactivatable bifunctional cross-linking agent 3'-arylazido-8-azidoadenosine 5'-triphosphate (diN(3)ATP) was used to investigate the spatial arrangement of the nucleotide binding sites of SecA, DiN(3)ATP is an authentic ATP analogue as it supports SecA-dependent precursor protein translocation and translocation ATPase, UV-induced photo-cross-linking of the diN(3)ATP-bound SecA results in the formation of stable dimeric s…

AzidesUltraviolet RaysProtein subunitATPaseDimerMutantPhotoaffinity LabelsBiologymedicine.disease_causeESSENTIAL COMPONENTenvironment and public healthBiochemistryBACILLUS-SUBTILISchemistry.chemical_compoundAdenosine TriphosphateBacterial ProteinsPROTON MOTIVE FORCEEscherichia colimedicinePRECURSOR PROTEIN TRANSLOCATIONNucleotideBinding siteEscherichia coliAdenosine Triphosphataseschemistry.chemical_classificationBinding SitesSecA ProteinsNucleotidesChemiosmosisEscherichia coli ProteinsMembrane Transport ProteinsPHOTOAFFINITY CROSS-LINKINGCross-Linking ReagentschemistryBiochemistryMEMBRANE-VESICLES REQUIRESPLASMA-MEMBRANE3'-ARYLAZIDO-BETA-ALANYL-8-AZIDO ATPCYTOPLASMIC MEMBRANEbiology.proteinPREPROTEIN TRANSLOCASEbacteriaDimerizationSEC Translocation ChannelsBiochemistry
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A multifuctional nanoplatform for drug targeted delivery based on radiation-engineered nanogels

2020

Abstract Under a rational design, combining biologically active molecules, ligands to specific cell receptors and fluorescent, radioactive or paramagnetic labels into a single nano-object can bridge the unique properties of the individual components and improve conventional sensing, imaging and therapeutic efficacies. The validation of these functional nano-objects requires careful testing both in terms of physico-chemical properties and biological behaviour in vitro and in vivo, prior to translation into the clinic. Ionising radiation of aqueous polymer solutions is a viable strategy to produce multifunctional nanogels from aqueous solutions of hydrophilic polymers. By proper selection of …

COLON-CANCER CELLSPULSE-RADIOLYSISDrugINDUCED CROSS-LINKINGSPECTRAL PROPERTIESmedia_common.quotation_subjectNanogelsConjugation reactionsNanotechnology01 natural sciencesAQUEOUS-SOLUTIONFLUORESCEIN030218 nuclear medicine & medical imagingNanogel03 medical and health sciences0302 clinical medicineHydrophilic polymers0103 physical sciencesNANOPARTICLESMoleculeIonising radiation synthesiIN-VIVOmedia_commonchemistry.chemical_classificationRadiationAqueous solution010308 nuclear & particles physicsIonising radiation synthesisRational designPolymerINSULINNanomedicineConjugation reactionchemistryDrug deliveryDrug deliveryNanomedicineSettore CHIM/07 - Fondamenti Chimici Delle TecnologieACID) NANOGELSRadiation Physics and Chemistry
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Biomimetic Alginate/Gelatin Cross-Linked Hydrogels Supplemented with Polyphosphate for Wound Healing Applications

2020

In the present study, the fabrication of a biomimetic wound dressing that mimics the extracellular matrix, consisting of a hydrogel matrix composed of non-oxidized and periodate-oxidized marine alginate, was prepared to which gelatin was bound via Schiff base formation. Into this alginate/oxidized-alginate-gelatin hydrogel, polyP was stably but reversibly integrated by ionic cross-linking with Zn2+ ions. Thereby, a soft hybrid material is obtained, consisting of a more rigid alginate scaffold and porous structures formed by the oxidized-alginate-gelatin hydrogel with ionically cross-linked polyP. Two forms of the Zn-polyP-containing matrices were obtained based on the property of polyP to f…

Keratinocyteszinc ionscell migrationMetal NanoparticlesPharmaceutical ScienceBiocompatible Materials02 engineering and technologyGelatinAnalytical ChemistryExtracellular matrixchemistry.chemical_compoundBiomimeticsCell MovementPolyphosphatesSpectroscopy Fourier Transform InfraredDrug DiscoveryalginateSkinchemistry.chemical_classificationcoacervate0303 health sciencesCoacervateTissue ScaffoldsHydrogelsPolymerHydrogen-Ion Concentration021001 nanoscience & nanotechnologyExtracellular MatrixZincChemistry (miscellaneous)Self-healing hydrogelsMolecular Medicine0210 nano-technologyHybrid materialPorosityinorganic polyphosphatefood.ingredientionic cross-linkingAlginatesCell Survivalperiodate oxidationArticlegelatinlcsh:QD241-44103 medical and health sciencesfoodlcsh:Organic chemistryHumansPhysical and Theoretical Chemistry030304 developmental biologyIonsWound HealingTissue EngineeringPolyphosphateOrganic Chemistryhuman epidermal keratinocytestechnology industry and agricultureChemical engineeringchemistrynanoparticlesEpidermisWound healingMolecules
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Off-Resonant Optical Excitation of Gold Nanorods: Nanoscale Imprint of Polarization Surface Charge Distribution

2011

International audience; We report on the nanoscale optical characterization of gold nanorods irradiated out of their plasmonic resonance. Our approach is based on the reticulation of a photopolymerizable formulation locally triggered by enhanced electromagnetic fields. The tiny local field enhancement stems from the surface polarization charges associated with the electric field discontinuity at the metal/dielectric interface. This allows us to get a nanoscale signature of the spatial distribution of the surface charge density in metallic nanoparticles irradiated off-resonance.

Materials sciencesurface charge densityAnalytical chemistryPhysics::Optics02 engineering and technologyDielectric010402 general chemistry01 natural sciencesplasmonicspolymer cross-linkingElectric fieldoptical properties of metal nanoparticlesGeneral Materials ScienceSurface chargePhysical and Theoretical ChemistryPolarization (electrochemistry)ComputingMilieux_MISCELLANEOUSPlasmonbusiness.industryCharge density[CHIM.MATE]Chemical Sciences/Material chemistry021001 nanoscience & nanotechnology0104 chemical sciences[ CHIM.POLY ] Chemical Sciences/Polymers[CHIM.POLY]Chemical Sciences/Polymers[ CHIM.MATE ] Chemical Sciences/Material chemistrypolymerizationOptoelectronicsNanorodnanorods0210 nano-technologybusinessExcitationThe Journal of Physical Chemistry Letters
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2,8-Diazido-ATP — a short-length bifunctional photoaffinity label for photoaffinity cross-linking of a stable F1 in ATP synthase (from thermophilic b…

1995

Abstract To demonstrate the direct interfacial position of nucleotide binding sites between subunits of proteins we have synthesized the bifunctional photoaffinity label 2,8-diazidoadenosine 5′-triphosphate (2,8-DiN3ATP). UV irradiation of the F1-ATPase (TF1) from the thermophilic bacterium PS3 in the presence of 2,8-DiN3ATP results in a nucleotide-dependent inactivation of the enzyme and in a nucleotide-dependent formation of α-β crosslinks. The results confirm an interfacial localization of all the nucleotide binding sites on TF1.

Models MolecularAzidesNucleotide binding siteLightStereochemistryImmunoblottingBiophysicsDirect interfacial localizationShort lengthBiochemistry8-azidoadenosine 5'-triphosphatechemistry.chemical_compoundAdenosine TriphosphateStructural BiologyGeneticsNucleotide binding sitesBifunctionalMolecular BiologyThermophilic bacterium PS3Photoaffinity cross-linkingchemistry.chemical_classificationATP synthasebiologyBacteriaThermophileAffinity LabelsCell BiologyProton-Translocating ATPasesEnzymeCross-Linking ReagentsBiochemistrychemistrybiology.proteinF1-ATPase: Short-length bifunctional photoaffinity labelFEBS Letters
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Hydration and water holding properties of cross-linked lignite humic acids

2014

Abstract Lignite and lignite humic acids, which are used as soil amendments sometimes, are supposed to improve soil properties such as water holding capacity. The structure of those materials is composed of various organic molecules stabilized mostly by weak interactions. Therefore, excess of water causes only partial swelling, but most of the physical structure is destabilized. This accelerates the desiccation and hampers their application as natural hydrogel-like substances. In order to stabilize the structure of lignite humic acids and improve the water holding capacity, we applied formaldehyde cross-linking procedure based on covalent coupling of aromatic humic acids moieties. By combin…

MoistureEnvironmental remediationChemistrySettore AGR/13 - Chimica AgrariaSoil ScienceSorptioncomplex mixturesSoil conditionerlignite humic acids cross-linking hydration DSC NMR relaxometry water molecule bridgesChemical engineeringSoil watermedicineOrganic chemistryRelative humiditySwellingmedicine.symptomThermal analysis
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Photoaffinity cross-linking of F1ATPase from spinach chloroplasts by 3'-arylazido-beta-alanyl-8-azido ATP.

1994

UV irradiation of the ATPase (CF1) from spinach chloroplasts in the presence of 3'-arylazido-beta-alanyl-8-azido ATP (8,3'-DiN3ATP) results in a nucleotide-dependent inactivation of the enzyme and in a nucleotide-dependent formation of alpha-beta cross-links. The results demonstrate an interfacial localization of the nucleotide binding sites on CF1.

Nucleotide binding siteAzidesChloroplastsStereochemistryPhotochemistryAffinity labelATPaseBiophysicsBiochemistryChloroplastF1ATPasechemistry.chemical_compoundAdenosine TriphosphateStructural BiologyVegetablesGeneticsBinding siteChenopodiaceaeInterfacial localizationMolecular BiologyPhotoaffinity cross-linkingchemistry.chemical_classificationbiologyfood and beveragesAffinity LabelsCell Biologybiology.organism_classificationChloroplastProton-Translocating ATPasesEnzymeCross-Linking Reagentschemistrybiology.proteinSpinach chloroplastAdenosine triphosphateFEBS letters
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