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564 results on '"Vianello, Fabio"'

153. Catalytically active bovine serum amine oxidase bound to fluorescent and magnetically drivable nanoparticles

Author

Sinigaglia,Giulietta, Magro,Massimiliano, Miotto,Giovanni, Cardillo,Sara, Agostinelli,Enzo, Zboril,Radek, Bidollari,Eris, Vianello,Fabio, Sinigaglia,Giulietta, Magro,Massimiliano, Miotto,Giovanni, Cardillo,Sara, Agostinelli,Enzo, Zboril,Radek, Bidollari,Eris, and Vianello,Fabio

Abstract

Giulietta Sinigaglia1, Massimiliano Magro1, Giovanni Miotto1, Sara Cardillo1, Enzo Agostinelli2,3, Radek Zboril4, Eris Bidollari2,3, Fabio Vianello11Department of Biological Chemistry, University of Padua, Padua, Italy; 2Istituto Pasteur-Fondazione Cenci Bolognetti, Department of Biochemical Sciences "A. Rossi Fanelli", SAPIENZA University of Rome, Rome, Italy; 3CNR, Institute Biology and Molecular Pathology, Rome, Italy; 4Regional Centre of Advanced Technologies and Materials, Department of Physical Chemistry, Palacky University, Olomouc, Czech RepublicAbstract: Novel superparamagnetic surface-active maghemite nanoparticles (SAMNs) characterized by a diameter of 10 ± 2 nm were modified with bovine serum amine oxidase, which used rhodamine B isothiocyanate (RITC) adduct as a fluorescent spacer-arm. A fluorescent and magnetically drivable adduct comprised of bovine serum copper-containing amine oxidase (SAMN–RITC–BSAO) that immobilized on the surface of specifically functionalized magnetic nanoparticles was developed. The multifunctional nanomaterial was characterized using transmission electron microscopy, infrared spectroscopy, mass spectrometry, and activity measurements. The results of this study demonstrated that bare magnetic nanoparticles form stable colloidal suspensions in aqueous solutions. The maximum binding capacity of bovine serum amine oxidase was approximately 6.4 mg g-1 nanoparticles. The immobilization procedure reduced the catalytic activity of the native enzyme to 30% ± 10% and the Michaelis constant was increased by a factor of 2. We suggest that the SAMN–RITC–BSAO complex, characterized by a specific activity of 0.81 IU g-1, could be used in the presence of polyamines to create a fluorescent magnetically drivable H2O2 and aldehydes-producing system. Selective tumor cell destruction is suggested as a potential future application of this system.Keywords: amine oxidase

Published
2012

155. Enzyme mimics complexing Cu(II) ion: structure-function relationships

Author

Corazza, A., Vianello, Fabio, Zennaro, Lucio, Gourova, N., DI PAOLO, MARIA LUISA, Signor, L., Marin, Oriano, Rigo, A., and Scarpa, M.

Subjects
Models, Molecular, Magnetic Resonance Spectroscopy, molecular modeling, Superoxide Dismutase, RESONANCE-SPECTRA, copper proteins, kinetics, peptide design, SUPEROXIDE-DISMUTASE, NMR spectroscopy, enzyme mimics, Ascorbic Acid, Catalysis, Structure-Activity Relationship, Thermodynamics, Amino Acid Sequence, Oxidation-Reduction, Copper, Chelating Agents
Abstract

Five peptides containing (His-X2)-His or (His-X3)-His motifs have been designed and synthesized to coordinate Cu(II). Structural information was obtained by various spectroscopic techniques and was used as constraint to search for local conformational energy minima by molecular mechanics. Thermodynamic stability constants of the Cu(II) chelates was obtained by 19F-NMR. The synthesized Cu(II)-peptide chelates were tested as catalysts of some important red-ox processes occuring in biological systems, in particular oxidation of ascorbate and dismutation of superoxide ion. The catalytic efficiency of the five chelates was much lower than that of ascorbate oxidase. On the contrary, two of them showed kinetic constants for superoxide dismutation about one order of magnitude lower than that of the enzyme Cu,Zn superoxide dismutase. In both cases, the catalytic properties were dependent on the peptide sequence. The relationships between structure and activity are discussed to find the structural parameters crucial for catalytic activity that can be modulated by appropriate design and synthesis of the peptides.

Published
1999

162. Colloidal Surface Active Maghemite Nanoparticles for Biologically Safe CrVI Remediation: from Core-Shell Nanostructures to Pilot Plant Development.

Author

Magro, Massimiliano, Domeneghetti, Stefania, Baratella, Davide, Jakubec, Petr, Salviulo, Gabriella, Bonaiuto, Emanuela, Venier, Paola, Malina, Ondřej, Tuček, Jiří, Ranc, Václav, Zoppellaro, Giorgio, Zbořil, Radek, and Vianello, Fabio

Subjects
TOXICOLOGY of chromium, MAGHEMITE, SURFACE active agents, SALMONELLA typhimurium, CHROMIUM in water, OXYANIONS, THERAPEUTICS
Abstract

The present study is aimed at the exploration of achievable improvements for CrVI ex situ and in situ water remediation by using novel naked colloidal maghemite (γ-Fe2O3) nanoparticles (surface active maghemite nanoparticles, SAMNs). The reliability of SAMNs for CrVI binding and removal was demonstrated, and SAMN@CrVI complex was characterized, as well as the covalent nature of the absorption was unequivocally proved. SAMNs were structurally and magnetically well conserved after CrVI binding. Thus, in consideration of their affinity for CrVI, SAMNs were exploited in a biological model system, mimicking a real in situ application. The assay evidenced a progressive reduction of revertant colonies of Salmonella typhimurium TA100 strain, as maghemite nanoparticles concentration increased, till the complete suppression of CrVI mutagen effect. Finally, an automatic modular pilot system for continuous magnetic removal and recovery of CrVI from water is proposed. SAMNs, thanks to their colloidal, binding, and catalytic properties, represent a promising tool as a reliable nanomaterial for water remediation by CrVI. [ABSTRACT FROM AUTHOR]

Published
2016
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163. Antioxidant compounds of organically and conventionally fertilized jambu (Acmella oleracea).

Author

da Silva Borges, Luciana, de Souza Vieira, Marizete Cavalcante, Vianello, Fabio, Goto, Rumy, and Pereira Lima, Giuseppina Pace

Subjects
ANTIOXIDANTS, ACMELLA, PHENOLS, CAROTENOIDS, ORGANIC farming
Abstract

Acmella oleracea (jambu), native to the Amazonas region (Brazil), has cosmetic and pharmacological properties, many of which are due to chemical components with antioxidant activity. Since organic cultivation has been reported to induce an increase in metabolic antioxidant components, this study aimed to determine the content of phenolic compounds, carotenoids, vitamin C, and polyamines, and the activity of peroxidase in two cultivars of jambu, Jambuarana, and Nazareth. Furthermore, leaves and inflorescences were studied to estimate the relative contribution of these tissues to the antioxidant potential of jambu. Organic farming induced higher levels of total phenolics and carotenoids in Jambuarana leaves and of spermidine and spermine in leaves and flowers of both the cultivars than conventional cultivation. Conventional fertilization led to nitrate accumulation in inflorescences and vitamin C in leaves, and to a higher total organic nitrogen content in jambu leaves and flowers than in organic cultivated plants. The fertilization procedures did not affect the activity of the enzyme peroxidase, but differences were observed between cultivars. [ABSTRACT FROM AUTHOR]

Published
2016
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164. Ternary Hybrid γ-Fe2O3/CrVI/Amine Oxidase Nanostructure for Electrochemical Sensing: Application for Polyamine Detection in Tumor Tissue.

Author

Bonaiuto, Emanuela, Magro, Massimiliano, Baratella, Davide, Jakubec, Petr, Sconcerle, Elisabetta, Terzo, Milo, Miotto, Giovanni, Macone, Alberto, Agostinelli, Enzo, Fasolato, Silvano, Venerando, Rina, Salviulo, Gabriella, Malina, Ondrej, Zboril, Radek, and Vianello, Fabio

Subjects
AMINE oxidase, NANOSTRUCTURES, BIOMACROMOLECULES, MAGHEMITE, HYDROGEN peroxide, ELECTROCHEMICAL sensors
Abstract

Dichromate binds to surface-active maghemite nanoparticles (SAMNs) to form a stable core-shell nanostructures (SAMN@CrVI). The hybrid was characterized by Mössbauer spectroscopy, high-angle annular dark-field imaging, electron energy-loss spectroscopy, and electrochemical techniques, which revealed a strong interaction of dichromate with the nanoparticle surface. Electrochemical characterization showed lower charge-transfer resistance, better electrochemical performance, and more reversible electrochemical behavior with respect to naked SAMNs. Moreover, SAMN@CrVI is an excellent electrocatalyst for hydrogen peroxide reduction. Furthermore, an enzyme, namely, bovine serum amine oxidase (BSAO: EC 1.4.3.6), was immobilized on SAMN@CrVI by self-assembly to give a ternary hybrid nanostructured catalyst for polyamine oxidation (SAMN@CrVI-BSAO). SAMN@CrVI-BSAO was applied for the development of a reagentless, fast, inexpensive, and interference-free polyamine biosensor, which was successfully exploited for the discrimination of tumorous tissue from healthy tissue in human crude liver extracts. [ABSTRACT FROM AUTHOR]

Published
2016
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174. ' Purification and characterization of amine oxidase from soy seedlings'

Author

Vianello, Fabio, DI PAOLO, MARIA LUISA, Gasparini, R., Stevanato, R., Scarpa, M., and AND RIGO, A.

Subjects
Amine oxidase, amine oxidase, Spermidine, polyamines, Size-exclusion chromatography, Biophysics, enzyme puification, enzyme kinetics, Inhibitors, affiniyt purification, Cyclohexylamine, Biochemistry, Chromatography, Affinity, Substrate Specificity, chemistry.chemical_compound, Affinity chromatography, Cadaverine, Putrescine, Enzyme kinetics, Amines, Amino Acids, Molecular Biology, Gel electrophoresis, Oxidoreductases Acting on CH-NH Group Donors, Chromatography, Electron Spin Resonance Spectroscopy, Amine oxidase (copper-containing), Chromatography, Ion Exchange, Molecular Weight, Kinetics, chemistry, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Amine Oxidase (Copper-Containing), Soybeans
Abstract

A simple and rapid procedure for purification of soybean seedling amine oxidase is reported. The crude enzyme, obtained by ammonium sulfate fractionation was purified by ion-exchange chromatography on a cellulose phosphate column and batch affinity chromatography on 6-aminohexyl-Sepharose. Cyclohexylamine, a competitive inhibitor, was utilized to elute the enzyme. A homogeneous enzyme was obtained with a yield higher than 25%, the content of minor components being < or = 2%. The M(r) estimated by gel filtration is 113,000 and 77,000 by sodium lauryl sulfate-polyacrylamide gel electrophoresis. The enzyme is a dimer and contains two Cu2+ ion per molecule. Its EPR spectrum is typical of Cu2+ in a tetragonal symmetry. The enzyme oxidizes cadaverine at high rate, the specific activity being 4.3 mukat/mg. Molecular, spectroscopic, and kinetic properties of this enzyme are reported.

Published
1993

177. Does the use of ozonized water influence the chemical characteristics of organic cabbage ( Brassica oleracea var. capitata)?

Author

Silva, Josiane, Costa, Sérgio, Oliveira, Luciana, Vieira, Marizete, Vianello, Fabio, and Lima, Giuseppina

Abstract

The aim of this study was to assess the influence of different cultivation procedures (conventional and organic), different sanitizers (ozone and chlorine) during the post-harvest storage of cabbages hybrid Fuyutoyo ( Brassica oleracea var. capitata). The cabbage plants were purchased directly from producers. At the end of the cropping cycle, which occurred 120 days after sowing, crop harvesting was carried out and the plants were immediately sanitized with water, chlorine and ozone. After cleansing, the cabbage plants were stored in a cooling chamber at 5 °C between 12 and 20 days. To predict the effect of commercialization, the cabbage head were removed between 12 and 20 days from the cooling chamber, one part was analyzed and the rest maintained in a local temperature (22 ± 2 °C) for 4 days. The biochemical analysis of the following were determined: total phenols, total flavonoids, vitamin C, total chlorophyll, nitrate, polyamines and antioxidant activity after 0, 12 and 20 days storage and 4 days at room temperature (12 + 4 and 20 + 4 days of storage), for market analysis. The biochemical analyses showed no statistical differences between conventional and organic cabbages. Thus, the consumption of organic or conventional cabbage provide the same content of antioxidant compounds analyzed and the sanitizing procedure (ozonated water ) did not modify the antioxidant capacity of the plant. [ABSTRACT FROM AUTHOR]

Published
2015
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183. Different pantoprazole therapy schedules in moderate-severe esophagitis

Author

Di Mario, Francesco, primary, Bo', Nadia Dal, additional, Germana', Bastianello, additional, Vianello, Fabio, additional, Marin, Renato, additional, Saggioro, Alfredo, additional, De Bastiani, Rudi, additional, Tafner, Giovanni, additional, Costan, Franco, additional, Valiante, Flavio, additional, Piazzi, Lucia, additional, Chilovi, Fausto, additional, Fedrizzi, Franco, additional, Marcon, Vincenzo, additional, Olivieri, Paolo, additional, Pieramico, Oreste, additional, Peri, Avetta, additional, and Leandro, Gioacchino, additional

Published
2003
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191. Kinetic role of a histidine residue in the T1 copper site of the laccase from Rigidoporus lignosus.

Author

Vianello, Fabio, Miotto, Giovanni, Cambria, Maria Teresa, Lima, Giuseppina P.P., Vanzani, Paola, and Di Paolo, Maria Luisa

Subjects
*RIGIDOPORUS lignosus, *HISTIDINE, *COPPER, *LACCASE, *FUNGAL enzymes, *DERIVATIZATION, *CATALYTIC activity, *PH effect
Abstract

Highlights: [•] The RIL activity at low pH value is controlled by an ionizable residue present in its active site. [•] DEPC derivatization of accessible His of RlL affect the kinetic behavior of RlL with pH and ionic strength. [•] Main role of His-457 in the control of the catalytic activity of laccase from Rigidoporus lignosus. [Copyright &y& Elsevier]

Published
2014
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194. Short-term treatment of gastric ulcer

Author

Mario, Francesco Di, primary, Battaglia, Giuseppe, additional, Leandro, Gioacchino, additional, Grasso, Giovanni, additional, Vianello, Fabio, additional, and Vigneri, Sergio, additional

Published
1996
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200. Serum pepsinogens as markers of Helicobacter pylori eradication

Author

Dotto, Paola, primary, Vianello, Fabio, additional, Plebani, Mario, additional, Ferrana, Marina, additional, Dal Bó, Nadia, additional, Del Bianco, Tiziana, additional, Salandin, Simonetta, additional, Basso, Daniela, additional, Leandro, Gioacchino, additional, Battaglia, Giuseppe, additional, and Di Mario, Francesco, additional

Published
1995
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