Sebastiano Vasi

Prof. Dr. Sebastiano Vasi

Dipartimento MIFT, Università degli Studi di Messina, 98166 Messina, Italy
orcid

Research Focus & Metrics

Academic Career Length

15Years (2012-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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8 March 2016 in Proceedings of the National Academy of Sciences
Verified
Journal Article
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Francesco MallamaceFrancesco Mallamace
Francesco Mallamace
Carmelo CorsaroCarmelo Corsaro
Carmelo Corsaro
Domenico MallamaceDomenico Mallamace
Domenico Mallamace
Sebastiano VasiSebastiano Vasi
Sebastiano Vasi
CVCirino Vasi
Cirino Vasi
H. Eugene StanleyH. Eugene Stanley
H. Eugene Stanley
We use 1H NMR to probe the energy landscape in the protein folding and unfolding process. Using the scheme <mml:math><mml:mo>⇄</mml:mo></mml:math>⇄ reversible unfolded (intermediate) <mml:math><mml:mo>→</mml:mo></mml:math>→ irreversible unfolded (denatured) state, we study the thermal denaturation of hydrated lysozyme that occurs when the temperature is increased. Using thermal cycles in the range <mml:math><mml:mrow><mml:mn>295</mml:mn><mml:mo><</mml:mo><mml:mi>T</mml:mi><mml:mo><</mml:mo><mml:mn>365</mml:mn></mml:mrow></mml:math>295<T<365 K and following different trajectories along the protein energy surface, we observe that the hydrophilic (the amide NH) and hydrophobic (methyl CH3 and methine CH) peptide groups evolve and exhibit different behaviors. We also discuss the role of water and hydrogen bonding in the protein configurational stability.

15 November 2014 in Computational and Structural Biotechnology Journal
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Journal Article
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Francesco MallamaceFrancesco Mallamace
Francesco Mallamace
Carmelo CorsaroCarmelo Corsaro
Carmelo Corsaro
Domenico MallamaceDomenico Mallamace
Domenico Mallamace
Sebastiano VasiSebastiano Vasi
Sebastiano Vasi
CVCirino Vasi
Cirino Vasi
GDGiacomo Dugo
Giacomo Dugo
The role the solvent plays in determining the biological activity of proteins is of primary importance. Water is the solvent of life and proteins need at least a water monolayer covering their surface in order to become biologically active. We study how the properties of water and the effect of its coupling with the hydrophilic moieties of proteins govern the regime of protein activity. In particular we follow, by means of Fourier Transform Infrared spectroscopy, the thermal evolution of the amide vibrational modes of hydrated lysozyme in the temperature interval 180 K < T < 350 K. In such a way we are able to observe the thermal limit of biological activity characterizing hydrated lysozyme. Finally we focus on the region of lysozyme thermal denaturation by following the evolution of the proton Nuclear Magnetic Resonance (NMR) spectra for 298 K < T < 366 K with the High-Resolution Magic Angle Spinning probe. Our data suggest that the hydrogen bond coupling between hydration water and protein hydrophilic groups is crucial in triggering the main mechanisms that define the enzymatic activity of proteins.

8 April 2014 in Nature Communications
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Journal Article
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MDM. G. Donato
M. G. Donato
JHJ. Hernandez
J. Hernandez
AMAlfredo Mazzulla
Alfredo Mazzulla
CPC. Provenzano
C. Provenzano
RSR. Saija
R. Saija
GCGabriella Cipparrone
Gabriella Cipparrone
Chirality is one of the most prominent and intriguing aspects of nature, from spiral galaxies down to aminoacids. Despite the wide range of living and non-living, natural and artificial chiral systems at different scales, the origin of chirality-induced phenomena is often puzzling. Here we assess the onset of chiral optomechanics, exploiting the control of the interaction between chiral entities. We perform an experimental and theoretical investigation of the simultaneous optical trapping and rotation of spherulite-like chiral microparticles. Due to their shell structure (Bragg dielectric resonator), the microparticles function as omnidirectional chiral mirrors yielding highly polarization-dependent optomechanical effects. The coupling of linear and angular momentum, mediated by the optical polarization and the microparticles chiral reflectance, allows for fine tuning of chirality-induced optical forces and torques. This offers tools for optomechanics, optical sorting and sensing and optofluidics.

8 August 2012 in Optics Letters
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Journal Article
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MDM. G. Donato
M. G. Donato
Sebastiano VasiSebastiano Vasi
Sebastiano Vasi
RSR. Sayed
R. Sayed
Philip JonesPhilip Jones
Philip Jones
FBFrancesco Bonaccorso
Francesco Bonaccorso
OMOnofrio Marago
Onofrio Marago
We use laser beams with radial and azimuthal polarization to optically trap carbon nanotubes. We measure force constants and trap parameters as a function of power showing improved axial trapping efficiency with respect to linearly polarized beams. The analysis of the thermal fluctuations highlights a significant change in the optical trapping potential when using cylindrical vector beams. This enables the use of polarization states to shape optical traps according to the particle geometry, as well as paving the way to nanoprobe-based photonic force microscopy with increased performance compared to a standard linearly polarized configuration.

12 February 2015 in Natural Product Research
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Journal Article
Closed access
Nicola CiceroNicola Cicero
Nicola Cicero
Carmelo CorsaroCarmelo Corsaro
Carmelo Corsaro
Andrea SalvoAndrea Salvo
Andrea Salvo
Sebastiano VasiSebastiano Vasi
Sebastiano Vasi
Salvatore GiofrèSalvatore Giofrè
Salvatore Giofrè
GDGiacomo Dugo
Giacomo Dugo
We have studied by means of High Resolution Magic Angle Spinning Nuclear Magnetic Resonance (HR-MAS NMR) the metabolic profile of the famous Sicilian lemon known as 'Interdonato Lemon of Messina PGI’. The PGI Interdonato Lemon of Messina possesses high organoleptic and healthy properties and is recognised as one of the most nutrient fruits. In particular, some of its constituents are actively studied for their chemo-preventive and therapeutic properties. In this paper, we have determined by means of HR-MAS NMR spectroscopy the molar concentration of the main metabolites constituent the juice of PGI Interdonato Lemon of Messina in comparison with that of the not-PGI Interdonato Lemon of Turkey. Our aim is to develop an analytical technique, in order to determine a metabolic fingerprint able to reveal commercial frauds in national and international markets.

1 October 2015 in Journal of Analytical Methods in Chemistry
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Carmelo CorsaroCarmelo Corsaro
Carmelo Corsaro
Domenico MallamaceDomenico Mallamace
Domenico Mallamace
Sebastiano VasiSebastiano Vasi
Sebastiano Vasi
GCGaetano Cammilleri
Gaetano Cammilleri
GDGiacomo Dugo
Giacomo Dugo
Nicola CiceroNicola Cicero
Nicola Cicero
NMR spectroscopy has become an experimental technique widely used in food science. The experimental procedures that allow precise and quantitative analysis on different foods are relatively simple. For a better sensitivity and resolution, NMR spectroscopy is usually applied to liquid sample by means of extraction procedures that can be addressed to the observation of particular compounds. For the study of semisolid systems such as intact tissues, High-Resolution Magic Angle Spinning (HR-MAS) has received great attention within the biomedical area and beyond. Metabolic profiling and metabolism changes can be investigated both in animal organs and in foods. In this work we present a proton HR-MAS NMR study on the typical vegetable foods of Mediterranean diet such as the Protected Geographical Indication (PGI) cherry tomato of Pachino, the PGI Interdonato lemon of Messina, several Protected Designation of Origin (PDO) extra virgin olive oils from Sicily, and the Traditional Italian Food Product (PAT) red garlic of Nubia. We were able to identify and quantify the main metabolites within the studied systems that can be used for their characterization and authentication.