0000000000066679

AUTHOR

Gerardo Palazzo

0000-0001-5504-2177

showing 6 related works from this author

Incorporation of the bacterial reaction centre into dendrimersomes

2012

For the first time the ability of the first generation dendrimer belonging to the family of polyester-benzylether, (3,5)12G1-PE-BMPA-(OH)4, to form dendrimersomes is presented together with their capability to reconstitute the integral membrane protein complex called Reaction Centre (RC) purified from the photosynthetic bacterium Rhodobacter sphaeroides. Size, polydispersity and time stability of the empty and protein containing dendrimersomes are presented together with the photochemical activity of the guest protein. The RC presence appears to strongly enhance the self-assembly properties of the Janus dendrimer, leading to the formation of proteo-dendrimersomes showing a photochemical act…

Liposomefood.ingredientbiologyChemistrycharge recombination; dendrimersomes; dynamic light scattering; integral proteins; self-aggregationbiology.organism_classificationLecithinCrystallographyRhodobacter sphaeroidesColloid and Surface ChemistryfoodDynamic light scatteringDocking (molecular)DendrimerSelf-assemblyta116Integral membrane proteinColloids and Surfaces A: Physicochemical and Engineering Aspects
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Probing light-induced conformational transitions in bacterial photosynthetic reaction centers embedded in trehalose-water amorphous matrices.

2004

Abstract The coupling between electron transfer and protein dynamics has been studied in photosynthetic reaction centers (RC) from Rhodobacter sphaeroides by embedding the protein into room temperature solid trehalose–water matrices. Electron transfer kinetics from the primary quinone acceptor (Q A − ) to the photoxidized donor (P + ) were measured as a function of the duration of photoexcitation from 20 ns (laser flash) to more than 1 min. Decreasing the water content of the matrix down to ≈5×10 3 water molecules per RC causes a reversible four-times acceleration of P + Q A − recombination after the laser pulse. By comparing the broadly distributed kinetics observed under these conditions …

Photosynthetic reaction centreLightPhotochemistryProtein ConformationKineticsPhotosynthetic Reaction Center Complex ProteinsBiophysicsAnalytical chemistryThermal fluctuationsPhotosynthetic reaction center; Trehalose; Electron transfer; Protein dynamics; Conformational relaxationProtein dynamicsRhodobacter sphaeroidesBiochemistryElectron transferElectron TransportRhodobacter sphaeroidesElectron transferSoft matterbiologyChemistryTrehaloseWaterCell Biologybiology.organism_classificationPhotosynthetic reaction centerConformational relaxationPhotoexcitationRelaxation (physics)Biochimica et biophysica acta
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Internal dynamics and protein-matrix coupling in trehalose-coated proteins.

2005

Abstract We review recent studies on the role played by non-liquid, water-containing matrices on the dynamics and structure of embedded proteins. Two proteins were studied, in water–trehalose matrices: a water-soluble protein (carboxy derivative of horse heart myoglobin) and a membrane protein (reaction centre from Rhodobacter sphaeroides ). Several experimental techniques were used: Mossbauer spectroscopy, elastic neutron scattering, FTIR spectroscopy, CO recombination after flash photolysis in carboxy-myoglobin, kinetic optical absorption spectroscopy following pulsed and continuous photoexcitation in Q B containing or Q B deprived reaction centre from R. sphaeroides . Experimental result…

Models MolecularAbsorption spectroscopyPhotosynthetic Reaction Center Complex ProteinsBiophysicsHemeRhodobacter sphaeroidesNeutron scatteringBiochemistryAnalytical Chemistrychemistry.chemical_compoundRhodobacter sphaeroidesMolecular dynamicsSpectroscopy Fourier Transform InfraredComputer SimulationMolecular Biologytrehalose protein simulation spectroscopyPhotolysisbiologyHydrogen bondMyoglobinTemperatureTrehaloseWaterHydrogen Bondingbiology.organism_classificationCrystallographyKineticsMyoglobinchemistryMembrane proteinFlash photolysisBiochimica et biophysica acta
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A Stereochemically Driven Supramolecular Polymerisation

2018

Anthracyclines self-assemble in water into dimers. In the presence of sufficiently high salt (NaCl) concentrations, solutions of the antibiotic doxorubicin, but not those of the closely related molecules daunomycin and epirubicin, turn into gels barely compatible with the presence of small oligomers. The use of spectroscopic, scattering, imaging and computational techniques, allowed light to be shed on the self-assembly process that triggered doxorubicin gelification. A complex picture emerged, with doxorubicin molecules assembled into long, highly chiral, supramolecular aggregates made of hundreds of units, showing redshifted fluorescence spectra, very short fluorescence lifetimes and smal…

Supramolecular chemistry02 engineering and technology010402 general chemistryPhotochemistrydoxorubicin01 natural sciencesCatalysisTurn (biochemistry)chemistry.chemical_compoundMolecular dynamicsanthracyclines; doxorubicin; fluorescence; circular dichroism; SAXS; molecular dynamicsMoleculeanthracyclinesScatteringOrganic ChemistrySAXSGeneral Chemistry021001 nanoscience & nanotechnologyFluorescencemolecular dynamicscircular dichroism0104 chemical sciencesMonomerchemistryPolymerizationfluorescence0210 nano-technologyChemistry - A European Journal
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The CdCl2 effects on synthetic DNAs encaged in the nanodomains of a cationic water-in-oil microemulsion

2011

The present work is dedicated to the study of the interactions of CdCl(2) with the synthetic polynucleotides polyAT and polyGC confined in the nanoscopic aqueous compartment of the water-in-oil microemulsion CTAB/pentanol/hexane/water, with the goal to mimic in vitro the situation met by the nucleic acids in vivo. In biological structures, in fact, very long strings of nucleic acids are segregated into very small compartments having a radius exceedingly smaller than the length of the encapsulated macromolecule. For comparison, the behaviour of polyGC was also studied in aqueous solutions of matched composition. The conformational and thermal stabilities of both polynucleotides enclosed in t…

inorganic chemicalsnanodomaincadmiumPolynucleotideswater-in-oil microemulsion; cadmium; model polynucleotidesGeneral Physics and AstronomyDissociation (chemistry)model polynucleotideschemistry.chemical_compoundCadmium ChlorideHexanesOrganic chemistryMicroemulsionPhysical and Theoretical ChemistryAqueous solutionconformational transitionCetrimoniumChemistryCationic polymerizationWaterDNAHexaneUV and CD spectroscopiesreverse micelleChemical engineeringwater-in-oil microemulsionPolynucleotideCetrimonium CompoundsNucleic acidCationic w/o microemulsionEmulsionssynthetic polynucleotideOilsMacromolecule
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The self-association equilibria of doxorubicin at high concentration and ionic strength characterized by fluorescence spectroscopy and molecular dyna…

2019

Abstract The self-association equilibria of doxorubicin hydrochloride (DX), at high drug and NaCl concentrations, are studied by temperature scan fluorescence spectroscopy, with the support of molecular dynamics (MD) calculations. Even though all anthracyclines show dimerization equilibria, DX only can further associate into long polymeric chains according to DXmon ⇄ DXdim ⇄ DXpol. This is reflected not only in the mechanical properties of DXpol solutions (behaving as thixotropic gels) but also in their spectroscopic behaviour. Fluorescence, in particular, is the technique of election to study this complex set of equilibria. Upon increasing the temperature, DXpol melts into DXdim, which in …

Dimer02 engineering and technologyfluorescence spectroscopy010402 general chemistry021001 nanoscience & nanotechnology01 natural sciencesFluorescenceFluorescence spectroscopymolecular dynamics0104 chemical sciencesTurn (biochemistry)chemistry.chemical_compoundMolecular dynamicsColloid and Surface ChemistryMonomerchemistryIonic strengthdoxorubicin self-associationMoleculePhysical chemistry0210 nano-technologyfluorescence spectroscopy; molecular dynamics; doxorubicin self-association
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