0000000000529685

AUTHOR

Lisa Elviri

showing 4 related works from this author

ETD and ECD Mass Spectrometry Fragmentation for the Characterization of Protein Post Translational Modifications

2012

The introduction of electron capture dissociation (ECD) by McLafferty and co-workers, and further of electron transfer dissociation (ETD), mechanism allows gas-phase fragmentation of multiply charged protein and peptide ions upon capture of a low-energy (<1 eV) electron or electron transfer in a gas phase ion-ion chemistry. The odd-electron species then undergoes rearrangement with subsequent cleavage of N−Cα backbone. Peptide fragmentation can take place inducing the formation of cand ztype fragment ions without loss of the information on the PTM localization. The key to the success of this approach is the selection of intact protein molecular ions and its profound potential for PTM charac…

Electron-transfer dissociationElectron transferSulfationFragmentation (mass spectrometry)Electron-capture dissociationChemistryBiophysicsPhosphorylationMass spectrometryIon
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Reactivity of anticancer metallodrugs with serum proteins: New insights from size exclusion chromatography-ICP-MS and ESI-MS

2010

International audience; A method based on the coupling of high resolution size-exclusion liquid chromatography using a polymer stationary phase with inductively coupled plasma mass spectrometry was developed to study the interactions of two metallodrugs - cisplatin and RAPTA-T - with the serum proteins albumin and transferrin. In contrast to previous approaches, the technique allowed the total recovery of the metals from the column and was able to discriminate between the different species of the metallodrugs and their complexes with the proteins at femtomolar detection levels. Metal binding was found to be dependent on the protein concentration and on the incubation time of the sample. Cis…

Binding-SitesElectrospray ionizationSize-exclusion chromatographyPeptidePlasma-Mass Spectrometry010402 general chemistry01 natural sciencesArticleAnalytical ChemistryOrganometallic Ruthenium CompoundCapillary electrophoresisComplexes[CHIM.ANAL]Chemical Sciences/Analytical chemistry[CHIM]Chemical SciencesInductively coupled plasma mass spectrometrySpectroscopychemistry.chemical_classificationChromatographyChemistry010401 analytical chemistryCisplatin BindingTransferrinAlbuminCapillary-ElectrophoresisMultidimensional Liquid-ChromatographyBlood proteins0104 chemical sciencesTransferrinPlatinum Antitumor ChemistryEscherichia-Coli
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Functional Fibronectin Adsorption on Aptamer-Doped Chitosan Modulates Cell Morphology by Integrin-Mediated Pathway.

2019

A decisive step in cell-biomaterial interaction is represented by the adsorption of proteins at the interface, whose fine control may be useful to trigger proper cell response. To this purpose, we can selectively control protein adsorption on biomaterials by means of aptamers. Aptamers selected to recognize fibronectin dramatically enhance chitosan ability to promote cell proliferation and adhesion, but the underlying biological mechanism remains unknown. We supposed that aptamers contributed to ameliorate the adsorption of fibronectin in an advantageous geometrical conformation for cells, thus regulating their morphology by the proper activation of the integrin-mediated pathway. We investi…

AptamerIntegrin02 engineering and technologyCell morphologylcsh:TechnologyArticle03 medical and health sciencesfibronectinGeneral Materials ScienceCytoskeletonlcsh:Microscopy030304 developmental biologylcsh:QC120-168.85cell morphology0303 health sciencesbiologylcsh:QH201-278.5ChemistryCell growthlcsh:TDNA aptamers; biomaterials; fibronectin; integrins; cell morphologyAdhesionDNA aptamers021001 nanoscience & nanotechnologyFibronectinlcsh:TA1-2040biology.proteinBiophysicsintegrinslcsh:Descriptive and experimental mechanicslcsh:Electrical engineering. Electronics. Nuclear engineering0210 nano-technologylcsh:Engineering (General). Civil engineering (General)lcsh:TK1-9971Protein adsorptionbiomaterialsMaterials (Basel, Switzerland)
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A Naturally Occurring Antibody Fragment Neutralizes Infectivity of Diverse Infectious Agents

2016

AbstractA phosphorylated peptide, named K40H, derived from the constant region of IgMs was detected in human serum by liquid chromatography coupled to high-resolution mass spectrometry. Synthetic K40H proved to exert a potent in vitro activity against fungal pathogens, and to inhibit HIV-1 replication in vitro and ex vivo. It also showed a therapeutic effect against an experimental infection by Candida albicans in the invertebrate model Galleria mellonella. K40H represents the proof of concept of the innate role that naturally occurring antibody fragments may exert against infectious agents, shedding a new light upon the posthumous role of antibodies and opening a new scenario on the multif…

0301 basic medicineMicrobial Sensitivity TestsVirus ReplicationArticleMass SpectrometryMicrobiology03 medical and health sciencesAnti-Infective AgentsCandida albicansHumansPhosphorylationCandida albicansInfectivityMultidisciplinaryInnate immune system030102 biochemistry & molecular biologybiologybiology.organism_classificationVirologyPeptide FragmentsIn vitroImmunoglobulin Fc FragmentsGalleria mellonella030104 developmental biologyImmunoglobulin MHumoral immunityHIV-1biology.proteinAntibodyEx vivoChromatography LiquidScientific Reports
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