Search results for "RGD"

showing 10 items of 81 documents

NMR Solution Structure of the Non-RGD Disintegrin Obtustatin

2003

The solution structure of obtustatin, a novel non-RGD disintegrin of 41 residues isolated from Vipera lebetina obtusa venom, and a potent and selective inhibitor of the adhesion of integrin alpha(1)beta(1) to collagen IV, has been determined by two-dimensional nuclear magnetic resonance. Almost the whole set of chemical shifts for 1H, 13C and 15N were assigned at natural abundance from 2D homonuclear and heteronuclear 500 MHz, 600 MHz and 800 MHz spectra at pH 3.0 recorded at 298 K and 303 K. Final structural constraints consisted of 302 non-redundant NOE (95 long-range, 60 medium, 91 sequential and 56 intra-residue), four disulfide bond distances, five chi1 dihedral angles and four hydroge…

Models MolecularProtein ConformationStereochemistryDisintegrinsMolecular Sequence DataStatic ElectricityViper VenomsDihedral angleCrystallography X-RayStructural BiologyDisintegrinAnimalsAmino Acid SequenceNuclear Magnetic Resonance BiomolecularMolecular BiologyProtein secondary structureConformational isomerismRGD motifMolecular StructureSequence Homology Amino AcidbiologyHydrogen bondChemistryCircular DichroismChemical shiftHydrogen BondingHydrogen-Ion ConcentrationSolutionsKineticsHeteronuclear moleculebiology.proteinOligopeptidesJournal of Molecular Biology
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BB0172, a Borrelia burgdorferi Outer Membrane Protein That Binds Integrin Α3Β1

2013

ABSTRACT Lyme disease is a multisystemic disorder caused by Borrelia burgdorferi infection. Upon infection, some B. burgdorferi genes are upregulated, including members of the microbial surface components recognizing adhesive matrix molecule (MSCRAMM) protein family, which facilitate B. burgdorferi adherence to extracellular matrix components of the host. Comparative genome analysis has revealed a new family of B. burgdorferi proteins containing the von Willebrand factor A (vWFA) domain. In the present study, we characterized the expression and membrane association of the vWFA domain-containing protein BB0172 by using in vitro transcription/translation systems in the presence of microsomal …

Models MolecularProtein familyMolecular Sequence DataIntegrinBiologyModels BiologicalMicrobiologyBiotecnologiaMicrobiologyAmino Acid SequenceBorrelia burgdorferiAdhesins BacterialMolecular BiologyIntegrin alpha3beta1Borrelia Burgdorferi InfectionProteïnes de membranaIntegrin alpha3beta1Articlesbiology.organism_classificationCell biologyBacterial adhesinBorrelia burgdorferibiology.proteinMSCRAMMBacterial outer membraneSequence AlignmentBacterial Outer Membrane ProteinsProtein Binding
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Tick-borne encephalitis virus, Borrelia burgdorferi sensu lato, Borrelia miyamotoi, Anaplasma phagocytophilum and Candidatus Neoehrlichia mikurensis …

2018

The aim of this study was to determine the occurrence of tick-borne pathogens of medical importance in questing ticks collected from five recreationally used islands along the Norwegian coastline. Furthermore, since coinfection may affect the disease severity, this study aimed to determine the extent of coinfection in individual ticks or co-localization of tick-borne pathogens. In all, 4158 questing Ixodes ricinus ticks were analyzed. For detection of tick-borne encephalitis virus (TBEV), nymphs (3690) were analyzed in pools of ten. To detect Borrelia burgdorferi sensu lato, B. miyamotoi, Anaplasma phagocytophilum and Candidatus Neoehrlichia mikurensis, 468 nymphs were analyzed individually…

Nymph0301 basic medicineIxodes ricinus030231 tropical medicine030106 microbiologySheep DiseasesBorrelia miyamotoiReal-Time Polymerase Chain ReactionMicrobiologyEncephalitis Viruses Tick-Borne03 medical and health sciences0302 clinical medicineBorrelia burgdorferi Groupparasitic diseasesPrevalencemedicineAnimalsHumansBorrelia burgdorferiNymphIslandsLyme DiseaseSheepIxodesbiologyCoinfectionNorwayBorreliaEhrlichiosisSequence Analysis DNAbacterial infections and mycosesbiology.organism_classificationmedicine.diseaseVirologyAnaplasma phagocytophilumTick-borne encephalitis virusInfectious DiseasesInsect ScienceCandidatusCoinfectionRecreationbacteriaParasitologyEncephalitis Tick-BorneAnaplasma phagocytophilumTicks and Tick-borne Diseases
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Polyaspartamide based hydrogel with cell recruitment properties for the local administration of hydrophobic anticancer drugs

2019

Abstract By exploiting the chemical versatility and the high water dispersibility of α,β-poly(N-2-hydroxyethyl)D,L-aspartamide, in this work, two different polymer derivatives were synthesized for the first time. Obtained macromolecules were characterized and used to produce hydrogels exploitable for the local release of hydrophobic anticancer drugs. The first derivative, bearing pendant β-cyclodextrins, was employed to solubilize tamoxifen, chosen as a model drug, and to produce a water soluble supramolecular complex, as evidenced through tamoxifen phase solubility studies. The second derivative, bearing pendant Cyclo(Arginine-Glyicine-Asparagine-D-Phenilyalanine-Cysteine) peptide moieties…

Polymers and PlasticsGeneral Chemical EngineeringSupramolecular chemistryPeptideRegional chemotherapymacromolecular substances02 engineering and technology010402 general chemistry01 natural sciencesBiochemistryMaterials ChemistryEnvironmental ChemistrySolubilityCytotoxicityPolyaspartamide RGD Hydrogel Regional chemotherapy Cell recruitmentchemistry.chemical_classificationRGDtechnology industry and agricultureGeneral Chemistry021001 nanoscience & nanotechnologyCell recruitmentCombinatorial chemistryIn vitro0104 chemical sciencesPolyaspartamideHydrogelchemistrySettore CHIM/09 - Farmaceutico Tecnologico ApplicativoCancer cellSelf-healing hydrogels0210 nano-technologyMacromoleculeReactive and Functional Polymers
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Conformation and concerted dynamics of the integrin-binding site and the C-terminal region of echistatin revealed by homonuclear NMR

2005

Copyright © by Portland Press. The final version of record is available at http://www.biochemj.org/bj/default.htm

Protein ConformationStereochemistryIntegrinNMR protein dynamics determinationTripeptideBiochemistryHomonuclear moleculeOff-resonance rotating-frame Overhauser enhancement spectroscopy (off-resonance ROESY)Protein structureSide chainAnimalsNuclear Magnetic Resonance BiomolecularMolecular BiologyIntegrin bindingRGD motifchemistry.chemical_classificationBinding Sites:CIENCIAS DE LA VIDA::Bioquímica [UNESCO]ChemistryEchistatin integrinSnakesUNESCO::CIENCIAS DE LA VIDA::BioquímicaCell BiologyRGD disintegrin; Echistatin; Integrin; NMR protein dynamics determination; Off-resonance rotating-frame Overhauser enhancement spectroscopy (off-resonance ROESY)Protein Structure TertiaryAmino acidRGD disintegrinDocking (molecular)EchistatinIntercellular Signaling Peptides and ProteinsPeptidesResearch ArticleProtein Binding
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Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection.

2019

The periplasmic lipoprotein BB0365 of the Lyme disease agent Borrelia burgdorferi is expressed throughout mammalian infection and is essential for all phases of Lyme disease infection; its function, however, remains unknown. In the current study, our structural analysis of BB0365 revealed the same structural fold as that found in the NqrC and RnfG subunits of the NADH:quinone and ferredoxin:NAD+ sodium-translocating oxidoreductase complexes, which points to a potential role for BB0365 as a component of the sodium pump. Additionally, BB0365 coordinated Zn2+ by the His51, His55, His140 residues, and the Zn2+ -binding site indicates that BB0365 could act as a potential metalloenzyme; therefore…

Protein FoldingProtein ConformationLipoproteinsBiophysicsBiochemistryMicrobiology03 medical and health sciencesLyme diseaseBacterial ProteinsStructural BiologyOxidoreductaseGeneticsmedicineHumansBinding siteBorrelia burgdorferiMolecular BiologyFerredoxin030304 developmental biologychemistry.chemical_classification0303 health sciencesLyme DiseaseBinding SitesbiologyChemistry030302 biochemistry & molecular biologyCell BiologyPeriplasmic spacebacterial infections and mycosesmedicine.diseasebiology.organism_classificationZincMembrane proteinBorrelia burgdorferiPeriplasmbacteriaNAD+ kinaseSodium-Potassium-Exchanging ATPaseFEBS lettersReferences
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CpG oligonukleotīdu pakošana RGD tripeptīdu saturošajās vīrusveidīgajās daļiņās

2015

Pasaulē ar hepatīta C vīrusu inficēto cilvēku skaits ir apmēram 170 miljoni, un pret HCV nav vakcīnas. Tāpēc ir svarīgi veikt pētījumus, kas saistīti ar vakcīnu izstrādi pret hepatīta C vīrusu. Darba mērķis bija veikt CpG oligodezoksinukleotīdu pakošanu vīrusveidīgajās daļiņās, kur kā nesējs tika izmantots 176 as garš hepatīta B kora modificēts proteīns. Nesēja galvenais imunodominantais rajons saturēja RGD tripeptīdu, un tā C gals bija sapludināts ar HCV NS3 222 – 251 as garu fragmentu. Tika attīrīti vairāki himēro HBc/HCV NS3 222 – 251 varianti. Tika veikta CpG oligodezoksinukleotīdu pakošana trīs dažādās ekspresijas plazmīdās. Pēc apstrādes ar DNāzi I tika konstatēts, ka vīrusveidīgo daļ…

RGDHBcVLPCpGHCVBioloģija
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Peptīdu lunasīna un RGD regulējošā darbība peļu šizofrēnijas modeļos

2018

Lunasīns ir bioloģiski aktīvs peptīds, kam piemīt antioksidatīvas, pretiekaisuma, pretvēža un holesterīna biosintēzi regulējošas īpašības. Nesen atklāts, ka tas spēj ietekmēt arī centrālo nervu sistēmu, izmainot peļu uzvedību, tādējādi radās interese pētīt lunasīna un tā sastāvā esošā tripeptīda RGD centrālos efektus. Maģistra darba mērķis bija pētīt intranazāli ievadītu peptīdu lunasīna un RGD darbību peļu šizofrēnijas modeļos, izmantojot atvērtā lauka testu un nosakot VMAT2 ekspresiju ar Western blot metodi. Iegūtie rezultāti rāda, ka gan lunasīns, gan RGD samazina amfetamīna un DOI izraisīto peļu horizontālo lokomotoro hiperaktivitāti, bet neietekmē fenciklidīna izraisīto vispārējo horiz…

RGDlokomotorā aktivitāteFarmācijaLunasīnscentrālā nervu sistēma
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Improving baculovirus transduction of mammalian cells by surface display of a RGD-motif

2006

An RGD-containing peptide, comprising 23 amino acids from the foot-and-mouth disease virus (FMDV) VP1 protein was engineered into the envelope of Autographa californica nuclear polyhedrosis virus surface (AcNPV) using two different display strategies. The RGD-motif is a well-described tripeptide, that by binding to cell surface integrins facilitates virus entry into cells. This epitope was displayed, either by directly modifying the native major envelope protein gp64 of AcNPV, or by incorporating a second, modified version of gp64 onto the virus surface. Transduction efficiencies of four mammalian cell lines were compared by detecting the expression of the reporter gene green fluorescent pr…

Reporter genebiologyvirusesAmino Acid MotifsGenetic VectorsBioengineeringGeneral Medicinebiology.organism_classificationApplied Microbiology and BiotechnologyMolecular biologyRecombinant ProteinsVirusEpitopeGreen fluorescent proteinViral ProteinsTransduction (genetics)Autographa californicaTransduction GeneticViral entryAnimalsHumansBaculoviridaeOligopeptidesBiotechnologyRGD motifJournal of Biotechnology
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Macroporous Scaffolds Based on Chitosan and Bioactive Molecules†

2007

Chitosan-based macroporous scaffolds for tissue engineering applications are developed by cryogelation in aqueous media. The cryogels obtained are modified using a new RGD-containing peptide developed in this laboratory. A RGD-containing peptide is chemically attached to the surface of the cryogels to improve cell adhesion to the 3D-structure chitosan-based scaffolds. The synthesis, physico-chemical, and biological evaluations of the system are described, and the optimization of the formulations is carried out by varying the reaction parameters. Fibroblasts and endothelial cells are used in cell cultures to determine cell behavior and the cytocompatibility of the macroporous cryogels. Cell …

ScaffoldPolymers and Plastics0206 medical engineeringCellBioengineeringPeptideNanotechnology02 engineering and technologyActin cytoskeleton organizationlaw.inventionScaffoldBiomaterialsChitosanchemistry.chemical_compoundTissue engineeringConfocal microscopylawMaterials ChemistrymedicineCell adhesionchemistry.chemical_classificationChitosanRGDChemistryCytocompatibility021001 nanoscience & nanotechnology020601 biomedical engineeringmedicine.anatomical_structureChemical engineering0210 nano-technologyCryogelsJournal of Bioactive and Compatible Polymers
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