Search results for "acrylamide"

showing 10 items of 485 documents

Self-Ordering Secondary Structure of d- and l-Arginine-Derived Polyamidoamino Acids

2017

This paper reports on synthesis, acid–base properties and pH-dependent structuring in water of d-, l- and d,l-ARGO7, bioinspired polymers obtained by polyaddition of the corresponding arginine stereoisomers with N,N′-methylenebis(acrylamide). The circular dichroism spectra of d- and l-ARGO7 showed a peak at 228 nm and quickly and reversibly responded to pH changes, but were nearly unaffected by temperature, ionic strength, and denaturating agents. Theoretical modeling studies of L-ARGO7 showed that it assumed a folded structure. Intramolecular interactions led to transoid arrangements of the main chain reminiscent of the protein hairpin motif. Torsion angles showed a quite similar distribut…

Materials Chemistry2506 Metals and AlloysMaterials scienceArgininePolymers and PlasticsStereochemistry02 engineering and technologyOrganic Chemistry; Polymers and Plastics; Inorganic Chemistry; Materials Chemistry2506 Metals and Alloys010402 general chemistry01 natural sciencesSpectral lineInorganic Chemistrychemistry.chemical_compoundMaterials ChemistryProtein secondary structurechemistry.chemical_classificationOrganic ChemistryPolymer021001 nanoscience & nanotechnology0104 chemical scienceschemistryChiral polymers polyamidoamino acids interpenetrating peptides self-structured polymersIonic strengthIntramolecular forceAcrylamide0210 nano-technologySelf ordering
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Degradable poly(amidoamine) hydrogels as scaffolds for in vitro culturing of peripheral nervous system cells.

2012

This paper reports on the synthesis and physico-chemical, mechanical, and biological characterization of two sets of poly(amidoamine) (PAA) hydrogels with potential as scaffolds for in vivo peripheral nerve regeneration. They are obtained by polyaddition of piperazine with N,N′-methylenebis(acrylamide) or 1,4-bis(acryloyl)piperazine with 1,2-diaminoethane as cross-linking agent and exhibit a combination of relevant properties, such as mechanical strength, biocompatibility, biodegradability, ability to induce adhesion and proliferation of Schwann cells (SCs) preserving their viability. Moreover, the most promising hydrogels, that is those deriving from 1,4-bis(acryloyl)piperazine, allow the …

Materials Chemistry2506 Metals and AlloysPoly(amidoamine)Cell SurvivalBioengineeringBiocompatible MaterialsNeural cell culturingPiperazinesRats Sprague-DawleyGanglia SpinalCell AdhesionPolyaminesAnimalsCell ProliferationNeuronsAcrylamidesPolymers and PlasticTissue EngineeringTissue ScaffoldsHydrogelsPolymer applicationEthylenediaminesBiomaterialNerve RegenerationRatsHydrogelBiodegradableSchwann CellsBiotechnologyMacromolecular bioscience
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Poly(N-isopropylacrylamide) and Copolymers: A Review on Recent Progresses in Biomedical Applications.

2017

The innate ability of poly(N-isopropylacrylamide) (PNIPAAm) thermo-responsive hydrogel to copolymerize and to graft synthetic polymers and biomolecules, in conjunction with the highly controlled methods of radical polymerization which are now available, have expedited the widespread number of papers published in the last decade—especially in the biomedical field. Therefore, PNIPAAm-based hydrogels are extensively investigated for applications on the controlled delivery of active molecules, in self-healing materials, tissue engineering, regenerative medicine, or in the smart encapsulation of cells. The most promising polymers for biodegradability enhancement of PNIPAAm hydrogels are probably…

Materials sciencePolymers and PlasticsBiocompatibilityPolymersRadical polymerizationthermo-responsive polymerBiocompatibilitatBioengineeringNanotechnology02 engineering and technologyReviewmacromolecular substances010402 general chemistry01 natural sciencesBiomaterialslcsh:Chemistrychemistry.chemical_compoundbiocompatibility:Enginyeria química [Àrees temàtiques de la UPC]Tissue engineeringlcsh:General. Including alchemybiodegradabilityPolymer chemistryCopolymerlcsh:Inorganic chemistrycopolymerspoly(N-isopropylacrylamide)lcsh:Sciencechemistry.chemical_classificationOrganic Chemistry4D-printingtechnology industry and agriculturePolymer021001 nanoscience & nanotechnologylcsh:QD146-1973. Good health0104 chemical sciencesCopolímerschemistrylcsh:QD1-999Self-healing hydrogelsPoly(N-isopropylacrylamide)lcsh:Q0210 nano-technologyEthylene glycollcsh:QD1-65Gels (Basel, Switzerland)
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Endocytotic uptake of HPMA-based polymers by different cancer cells: impact of extracellular acidosis and hypoxia.

2017

Daniel Gündel,1 Mareli Allmeroth,2 Sarah Reime,1 Rudolf Zentel,2 Oliver Thews1 1Institute of Physiology, Martin Luther University Halle-Wittenberg, Halle (Saale), 2Institute of Organic Chemistry, Johannes Gutenberg-University, Mainz, Germany Background: Polymeric nanoparticles allow to selectively transport chemotherapeutic drugs to the tumor tissue. These nanocarriers have to be taken up into the cells to release the drug. In addition, tumors often show pathological metabolic characteristics (hypoxia and acidosis) which might affect the polymer endocytosis.Materials and methods: Six different N-(2-hydroxypropyl)methacrylamide (HPMA)-based polymer structures (homopolymer as well as…

Materials sciencePolymersBiophysicsHPMA–LMA copolymersPharmaceutical ScienceBioengineering02 engineering and technologyEndocytosisMethacrylatestructure–property relationshipBiomaterials03 medical and health scienceschemistry.chemical_compound0302 clinical medicineDrug Delivery SystemsInternational Journal of NanomedicineCell Line TumorDrug Discoverytumor linesMethacrylamideAnimalstumor microenvironmentOriginal ResearchAcrylamidesTumor hypoxiaPinocytosisOrganic ChemistryGeneral MedicineHydrogen-Ion Concentration021001 nanoscience & nanotechnologyEndocytosisRatsMolecular WeightBiochemistrychemistry030220 oncology & carcinogenesisDrug deliveryCancer cellMethacrylatesNanoparticlesTumor HypoxiaNanocarriers0210 nano-technologyAcidosisHydrophobic and Hydrophilic InteractionsInternational journal of nanomedicine
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HPMA-based block copolymers promote differential drug delivery kinetics for hydrophobic and amphiphilic molecules.

2015

Abstract We describe a method how polymeric nanoparticles stabilized with (2-hydroxypropyl)methacrylamide (HPMA)-based block copolymers are used as drug delivery systems for a fast release of hydrophobic and a controlled release of an amphiphilic molecule. The versatile method of the miniemulsion solvent-evaporation technique was used to prepare polystyrene (PS) as well as poly-d/l-lactide (PDLLA) nanoparticles. Covalently bound or physically adsorbed fluorescent dyes labeled the particles’ core and their block copolymer corona. Confocal laser scanning microscopy (CLSM) in combination with flow cytometry measurements were applied to demonstrate the burst release of a fluorescent hydrophobic…

Materials sciencePolymersPolyestersBiomedical EngineeringNanoparticleFluorescent Antibody TechniqueNanotechnology02 engineering and technology010402 general chemistry01 natural sciencesBiochemistryBiomaterialschemistry.chemical_compoundSurface-Active AgentsDrug Delivery SystemsAmphiphileCopolymerMethacrylamideHumansMolecular BiologyDrug CarriersGeneral MedicineLipid Droplets021001 nanoscience & nanotechnologyControlled release0104 chemical sciencesMiniemulsionDrug LiberationKineticschemistryDrug deliveryBiophysicsMethacrylatesNanoparticlesPolystyrenesNanocarriers0210 nano-technologyHydrophobic and Hydrophilic InteractionsBiotechnologyHeLa CellsActa biomaterialia
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Multifunctional clickable and protein-repellent magnetic silica nanoparticles

2016

Silica nanoparticles are versatile materials whose physicochemical surface properties can be precisely adjusted. Because it is possible to combine several functionalities in a single carrier, silica-based materials are excellent candidates for biomedical applications. However, the functionality of the nanoparticles can get lost upon exposure to biological media due to uncontrolled biomolecule adsorption. Therefore, it is important to develop strategies that reduce non-specific protein-particle interactions without losing the introduced surface functionality. Herein, organosilane chemistry is employed to produce magnetic silica nanoparticles bearing differing amounts of amino and alkene func…

Materials scienceSurface PropertiesSilicon dioxideNanoparticleNanotechnology02 engineering and technology010402 general chemistry01 natural sciencesMagneticschemistry.chemical_compoundAdsorptionDynamic light scatteringAnimalsGeneral Materials Sciencechemistry.chemical_classificationBiomoleculeSerum Albumin BovineSilicon Dioxide021001 nanoscience & nanotechnologyDynamic Light ScatteringFerrosoferric Oxide0104 chemical sciencesElectrophoresischemistryCovalent bondThermogravimetryNanoparticlesPolystyrenesCattleElectrophoresis Polyacrylamide GelMuramidaseAdsorption0210 nano-technologyProtein adsorptionNanoscale
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Identification of a 49-kDa hydrophobic cell wall mannoprotein present in velum yeast which may be implicated in velum formation

2000

Analysis of velum-forming yeast cell wall components released by beta-1,3-glucanase treatment were compared with those of a non velum-forming yeast. SDS-PAGE electrophoresis and Western blotting with ConA-peroxidase staining of mannoproteins allowed us to identify a 49-kDa mannoprotein present in the cell wall of the velum-forming yeast and hardly visible in the control. The cell wall nature of this protein was confirmed by labelling with the non-permeable sulfosuccinimydiyl-6-(biotinamido)hexanoate reagent. A partial purification of this mannoprotein by anion exchange HPLC followed by surface hydrophobicity determination revealed that the fraction containing the 49-kDa mannoprotein was the…

Membrane GlycoproteinsSurface PropertiesBlotting WesternCellWineSaccharomyces cerevisiaeBiologyMicrobiologyYeastStainingFungal Proteinscarbohydrates (lipids)BlotCell wallElectrophoresismedicine.anatomical_structureBiochemistryCell WallBiotinylationGeneticsmedicineBiotinylationElectrophoresis Polyacrylamide GelMolecular BiologyPolyacrylamide gel electrophoresisFEMS Microbiology Letters
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Charge Pair Interactions in Transmembrane Helices and Turn Propensity of the Connecting Sequence Promote Helical Hairpin Insertion

2013

alpha-Helical hairpins, consisting of a pair of closely spaced transmembrane (TM) helices that are connected by a short interfacial turn, are the simplest structural motifs found in multi-spanning membrane proteins. In naturally occurring hairpins, the presence of polar residues is common and predicted to complicate membrane insertion. We postulate that the pre-packing process offsets any energetic cost of allocating polar and charged residues within the hydrophobic environment of biological membranes. Consistent with this idea, we provide here experimental evidence demonstrating that helical hairpin insertion into biological membranes can be driven by electrostatic interactions between clo…

Models MolecularBioquímicaProtein FoldingGlycosylationMolecular Sequence Datamembrane integrationEndoplasmic Reticulumsalt bridgeProtein Structure SecondaryTurn (biochemistry)Viral Proteins03 medical and health sciencesProtein structureStructural BiologyComputer SimulationAmino Acid SequenceAmino AcidsStructural motifMolecular Biologytranslocon030304 developmental biology0303 health sciencesBinding SitesChemistry030302 biochemistry & molecular biologyProteïnes de membranaBiochemistry and Molecular BiologyMembrane ProteinsBiological membraneTransloconelectrostatic interactionsTransmembrane proteinProtein Structure TertiaryPoliovirusProtein TransportCrystallographyTransmembrane domainhelical hairpinMembrane proteinMutationBiophysicsElectrophoresis Polyacrylamide GelHydrophobic and Hydrophilic InteractionsBiokemi och molekylärbiologi
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Design and construction of highly stable, protease-resistant chimeric avidins.

2005

The chicken avidin gene family consists of avidin and seven separate avidin-related genes (AVRs) 1-7. Avidin protein is a widely used biochemical tool, whereas the other family members have only recently been produced as recombinant proteins and characterized. In our previous study, AVR4 was found to be the most stable biotin binding protein thus far characterized (T(m) = 106.4 degrees C). In this study, we studied further the biotin-binding properties of AVR4. A decrease in the energy barrier between the biotin-bound and unbound state of AVR4 was observed when compared with that of avidin. The high resolution structure of AVR4 facilitated comparison of the structural details of avidin and …

Models MolecularBiotin bindingInsectaProtein familyProtein subunitRecombinant Fusion ProteinsMolecular Sequence DataBiotinBiosensing TechniquesBiologyProtein EngineeringBiochemistryProtein Structure SecondaryProtein structureAnimalsAmino Acid SequenceMolecular BiologyThermostabilityCalorimetry Differential ScanningSequence Homology Amino AcidTemperatureCell BiologyProtein engineeringAvidinRecombinant ProteinsProtein Structure TertiaryKineticsBiochemistryMicroscopy FluorescenceMutagenesisBiotinylationMutationbiology.proteinChromatography GelThermodynamicsElectrophoresis Polyacrylamide GelEndopeptidase KBaculoviridaeChickensAvidinChromatography LiquidPeptide HydrolasesProtein BindingThe Journal of biological chemistry
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Construction of a dual chain pseudotetrameric chicken avidin by combining two circularly permuted avidins.

2004

Two distinct circularly permuted forms of chicken avidin were designed with the aim of constructing a fusion avidin containing two biotin-binding sites in one polypeptide. The old N and C termini of wild-type avidin were connected to each other via a glycine/serine-rich linker, and the new termini were introduced into two different loops. This enabled the creation of the desired fusion construct using a short linker peptide between the two different circularly permuted subunits. The circularly permuted avidins (circularly permuted avidin 5 → 4 and circularly permuted avidin 6 → 5) and their fusion, pseudotetrameric dual chain avidin, were biologically active, i.e. showed biotin binding, and…

Models MolecularBiotin bindingProtein DenaturationProtein FoldingStereochemistryProtein ConformationProtein subunitMolecular Sequence DataGlycineBiotinBiochemistrySensitivity and SpecificityProtein Structure Secondarystomatognathic systemChain (algebraic topology)SerineAnimalsAmino Acid SequenceBinding siteProtein Structure QuaternaryMolecular BiologyLinker peptideBinding SitesbiologyCell Biologyrespiratory systemAvidinProtein Structure TertiaryCrystallographyKineticsMutationbiology.proteinChromatography GelElectrophoresis Polyacrylamide GelEndopeptidase KPeptidesLinkerChickensAvidinProtein BindingThe Journal of biological chemistry
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