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213. Isolation and full characterisation of a potentially allergenic lipid transfer protein (LTP) in almond.

Author

Buhler, Sofie, Tedeschi, Tullia, Faccini, Andrea, Garino, Cristiano, Arlorio, Marco, Dossena, Arnaldo, and Sforza, Stefano

Subjects
LIPID transfer protein, ALMOND, ALLERGENS, CYSTEINE, DISULFIDES, LIQUID chromatography-mass spectrometry, CHEMICAL reduction
Abstract

Non-specific lipid transfer proteins (nsLTP) were shown to be among the most significant allergens, in particular in several fruits belonging to the Rosaceae family. The molecular features of LTPs, such as the presence of eight cysteine residues forming four disulfide bridges, confer a compact structure, decreasing the probability of degradation due to cooking or digestion, thereby increasing the chance of systemic absorption and severe allergic reactions. Few studies on LTP-induced allergies regarding almond (Prunus dulcisL) are available in the literature. In the present work, we describe for the first time the extraction and purification of an almond LTP, achieving its full characterisation by using liquid chromatography and exact mass spectrometry; the full sequence was identified by means of LC-ESI-Orbitrap™-MS applying a bottom-up approach. The characterised protein consists of 92 amino acids and has a calculated exact MW of 9579.0. The presence of four disulfide bridges was confirmed after reduction, as shown by a mass increment of 8 Da. Finally, its potential allergenicity was confirmed via anin silicoapproach. The results presented here demonstrate the enormous potential of advanced MS techniques for obtaining high-quality structural and functional data of allergenic proteins in a short time. [ABSTRACT FROM PUBLISHER]

Published
2015
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222. Anti-gene peptide nucleic acid specifically inhibits MYCN expression in human neuroblastoma cells leading to cell growth inhibition and apoptosis

Author

Tonelli, Roberto, primary, Purgato, Stefania, additional, Camerin, Consuelo, additional, Fronza, Raffaele, additional, Bologna, Fabrizio, additional, Alboresi, Simone, additional, Franzoni, Monica, additional, Corradini, Roberto, additional, Sforza, Stefano, additional, Faccini, Andrea, additional, Shohet, Jason M., additional, Marchelli, Rosangela, additional, and Pession, Andrea, additional

Published
2005
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232. Targeted inhibition of NMYC by peptide nucleic acid in N-myc amplified human neuroblastoma cells: cell-cycle inhibition with induction of neuronal cell differentiation and apoptosis

Author

Pession, Andrea, primary, Tonelli, Roberto, additional, Fronza, Raffaele, additional, Sciamanna, Elena, additional, Corradini, Roberto, additional, Sforza, Stefano, additional, Tedeschi, Tullia, additional, Marchelli, Rosangela, additional, Montanaro, Lorenzo, additional, Camerin, Consuelo, additional, Franzoni, Monica, additional, and Paolucci, Guido, additional

Published
2004
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249. Introducing enzyme selectivity: a quantitative parameter to describe enzymatic protein hydrolysis.

Author

Sforza, Stefano, Butré, Claire, Gruppen, Harry, and Wierenga, Peter

Subjects
*PROTEIN hydrolysates, *LIQUID chromatography-mass spectrometry, *ENZYMES, *WHEY proteins, *BACILLUS licheniformis
Abstract

Enzyme selectivity is introduced as a quantitative parameter to describe the rate at which individual cleavage sites in a protein substrate are hydrolyzed relative to other cleavage sites. Whey protein isolate was hydrolyzed by Bacillus licheniformis protease, which is highly specific for Glu and Asp residues. The molar concentration of all peptides (58) from β-lactoglobulin formed during hydrolysis was determined from the UV signal. The quality of identification and quantification of the peptides were described by newly defined parameters: the peptide sequence coverage (on average 94 %) and the molar sequence coverage (on average 75 %). The selectivity was calculated from the rate of hydrolysis of each cleavage site, and showed differences of up to a factor of 5,000. The ability to quantitatively discriminate the enzyme preference towards individual cleavage sites is considered essential to the understanding of enzymatic protein hydrolysis. [Figure not available: see fulltext.] [ABSTRACT FROM AUTHOR]

Published
2014
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250. Optical and dielectric sensors based on antimicrobial peptides for microorganism diagnosis.

Author

Bauer, Margaret E., Dutta, Noton Kumar, Sforza, Stefano, and Igbinosa, Etinosa

Subjects
ANTIMICROBIAL peptides, BIOSENSORS, BACTERIAL diseases, IMPEDANCE spectroscopy, FLUORESCENCE spectroscopy
Abstract

Antimicrobial peptides (AMPs) are natural compounds isolated from a wide variety of organisms that include microorganisms, insects, amphibians, plants, and humans. These biomolecules are considered as part of the innate immune system and are known as natural antibiotics, presenting a broad spectrum of activities against bacteria, fungi, and/or viruses. Technological innovations have enabled AMPs to be utilized for the development of novel biodetection devices. Advances in nanotechnology, such as the synthesis of nanocomposites, nanoparticles, and nanotubes have permitted the development of nanos-tructured platforms with biocompatibility and greater surface areas for the immobilization of biocomponents, arising as additional tools for obtaining more efficient biosensors. Diverse AMPs have been used as biological recognition elements for obtaining biosensors with more specificity and lower detection limits, whose analytical response can be evaluated through electrochemical impedance and fluorescence spectroscopies. AMP-based biosensors have shown potential for applications such as supplementary tools for conventional diagnosis methods of microorganisms. In this review, conventional methods for microorganism diagnosis as well new strategies using AMPs for the development of impedimetric and fluorescent biosensors are highlighted. AMP-based biosensors show promise as methods for diagnosing infections and bacterial contaminations as well as applications in quality control for clinical analyses and microbiological laboratories. [ABSTRACT FROM AUTHOR]

Published
2014
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