Fabrizio Alfieri

Publications (2) View all

• Article: Structural and Thermal Stability Characterization of Escherichia colid‐Galactose/d‐Glucose‐Binding Protein

  Sabato d'Auria, Fabrizio Alfieri, Maria Staiano, Fabrizio Pelella, Mose' Rossi, Andrea Scirè, Fabio Tanfani, Enrico Bertoli, Zigmunt Grycznyski, Joseph R. Lakowicz
  [show abstract] [hide abstract]
  ABSTRACT: The effect of temperature and glucose binding on the structure of the galactose/glucose-binding protein from Escherichia coli was investigated by circular dichroism, Fourier transform infrared spectroscopy, and steady-state and time-resolved fluorescence. The data showed that the glucose binding induces a moderate change of the secondary structure content of the protein and increases the protein thermal stability. The infrared spectroscopy data showed that some protein stretches, involved in α-helices and β strand conformations, are particularly sensitive to temperature. The fluorescence studies showed that the intrinsic tryptophanyl fluorescence of the protein is well represented by a three-exponential model and that in the presence of glucose the protein adopts a structure less accessible to the solvent. The new insights on the structural properties of the galactose/glucose-binding protein can contribute to a better understanding of the protein functions and represent fundamental information for the development of biotechnological applications of the protein.
  Biotechnology Progress 09/2008; 20(1):330 - 337. · 2.34 Impact Factor
• Article: Structural and thermal stability characterization of Escherichia coli D-galactose/D-glucose-binding protein.

  Sabato D'Auria, Fabrizio Alfieri, Maria Staiano, Fabrizio Pelella, Mose' Rossi, Andrea Scirè, Fabio Tanfani, Enrico Bertoli, Zigmunt Grycznyski, Joseph R Lakowicz
  [show abstract] [hide abstract]
  ABSTRACT: The effect of temperature and glucose binding on the structure of the galactose/glucose-binding protein from Escherichia coli was investigated by circular dichroism, Fourier transform infrared spectroscopy, and steady-state and time-resolved fluorescence. The data showed that the glucose binding induces a moderate change of the secondary structure content of the protein and increases the protein thermal stability. The infrared spectroscopy data showed that some protein stretches, involved in alpha-helices and beta strand conformations, are particularly sensitive to temperature. The fluorescence studies showed that the intrinsic tryptophanyl fluorescence of the protein is well represented by a three-exponential model and that in the presence of glucose the protein adopts a structure less accessible to the solvent. The new insights on the structural properties of the galactose/glucose-binding protein can contribute to a better understanding of the protein functions and represent fundamental information for the development of biotechnological applications of the protein.
  Biotechnology Progress 20(1):330-7. · 2.34 Impact Factor