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Danilo Milardi Personal Page

by · March 27, 2019

E-mail: danilo.milardiATic.cnr.it
Address: CNR – Institute of Crystallography, Via Paolo Gaifami 18, 95126 Catania, Italy

Present Position:

-Researcher

Curriculum Vitae :

Education

1986-1992     Degree in Industrial Chemistry, University of Catania, Italy

1993-1996     PhD in Physical Chemistry, University of Catania, Italy

Career

1996-1999     Research fellow  at Wyeth-Lederle, Catania Plant.

1996-2001     Research collaborator, Department of Chemical Sciences, University of Catania, Italy

2001-present  Researcher, (National Research Council) CNR, Italy.

2015-present  Lecturer of the international school of doctorate in Chemical Sciences of the University of Catania.

During the academic years 2001-2002, 2002-2003, 2007-2008 and 2008-2009 he is lecturer of Physical-Chemistry and General-Inorganic Chemistry at the University of Catania. He is responsible of the training plan of the public-private Lab CNR-Wyeth Lederle n° DM20919. He is the coordinator of the RSTL research project n° 620 financially supported by CNR and of local coordinator of a PRIN 2015 project. He has been member of the organizing committee of several national and international congresses. He has been invited speaker in several national and international symposia. He is author of 94 peer-reviewed papers and 5 book chapters.

Research Activity:

My broad goal is to discover how intra- and inter-molecular interactions lead to the emergence of protein/nucleic acids/lpid properties and biological function by combining calorimetric and spectroscopic experiments with dynamics simulations. A major focus is to achieve new insights into functional molecular mechanisms regulating protein folding/assembly, protein-protein and protein – membrane interactions with the ultimate goal of understanding how microscopic events may lead to eventually pathogenic consequences at a molecular level. The adverse effects of abnormal environmental factors (e.g. metal ions, lipid membranes and oxidative stress) on the structure, stability and function of different biomolecular assemblies fall within my field of interest.

Specific areas of interest are:

  1. Spectroscopic and calorimetric analysis of two-state and downhill protein folding.
  2. Stability of nucleic acid structures i.e. G-quadruplexes and circulating miRNAs.
  3. Amyloid aggregation and membrane leakage assays.
  4. Proteasome and ubiquitin activity.
  5. Ligand – protein interactions.

Applications range from the preparation of lipid-based drug delivery systems, to the design of small molecules acting as proteostasis regulators for the treatment of cancer and neurodegenerative disorders.

Selected publications: (max 5)

1) D. Milardi, F. Arnesano, G. Grasso, A. Magrì, G. Tabbì, S. Scintilla, G. Natile* and E. Rizzarelli*, Ubiquitin Stability and Lys63-Linked Polyubiquitination Sites are Compromised on Copper Binding, Angewandte Chemie Int. Ed., 2007, 46, 7993-7995.

2) A. M. Santoro, M.C. Lo Giudice, A. D’Urso, R. Lauceri, R. Purrello,* and Danilo Milardi*, Cationic Porphyrins Are Reversible Proteasome Inhibitors, J. Am. Chem. Soc., 2012, 134, 10451−10457.

3) M. Palmieri, G. Malgieri, L. Russo, I. Baglivo, S. Esposito, F. Netti, A. Del Gatto, I. de Paola, L. Zaccaro, P.V. Pedone, C. Isernia, D. Milardi and R. Fattorusso*, Structural Zn(II) Implies a Switch from Fully Cooperative to Partly Downhill Folding in Highly Homologous Proteins, J. Am. Chem. Soc. 2013, 135, 5220−5228.

4) G. Grasso, A. M. Santoro, V. Lanza, D. Sbardella, G.R. Tundo, C. Ciaccio, S. Marini, M. Coletta, D. Milardi*, The double faced role of copper in Ab homeostasis: A survey on the interrelationship between metal dyshomeostasis, UPS functioning and autophagy in neurodegeneration. Coordination Chemistry Reviews, 2017, 347, 1–22.

5) F. Bellia, V. Lanza, S. Garcıa-Vinuales, I. M. M. Ahmed, A. Pietropaolo, C. Iacobucci, G. Malgieri, G. D’Abrosca, R. Fattorusso, V. G. Nicoletti, D. Sbardella, G. R. Tundo, M. Coletta, L. Pirone, E. Pedone, D. Calcagno, G. Grasso* and D. Milardi*, Ubiquitin binds the amyloid b peptide and interferes with its clearance pathways, Chem. Sci. (2019), 10, 2732-2742.