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Claudio Canale

Affiliated Researcher
Researcher

Research Line

Nanoscopy & NIC@IIT

Center

IIT Central Research Labs Genova

Contacts

via Morego 30
+39 010 71781 885
Contact Me

About

 

Claudio Canale is Team Leader at the Department of Nanophysics at the Istituto Italiano di Tecnologia (IIT). His activity is mainly focused on the application of scanning probe techniques in the study of bio-materials and bio-mechanisms. He graduated in Physics in at the University of Genova (Italy) in 2001, studying the distribution of scalar fields in the atmosphere, with particular interest on the saturation of intermittency in the temperature and humidity fields. He collaborated with the National Institute of Physics of Matter (2001-2002) on in the development of selective sensors for water analysis; functionalized self-assembled monolayers of thiols on gold were used for the detection of heavy ions in water. In 2006 he received the Ph.D. from the University of Genova, defending a thesis on the characterization of misfolded protein aggregates. The topics of his research are on the biological application of the AFM. In particular, he studied the kinetics of aggregation of different amyloidogenic peptides, relating them to the different condition at which the aggregation occured. He studied the interaction between amyloid aggregates and other bio-materials, with a particular interest on the interaction of amyloid olygomers and model membranes. In the last years he moved his interest also on the AFM application on cell, he is working at the study of cell mechanics, he focused in particular in the study of cell nuclei mechanics. He is interested in cell adhesion mechanism and he developed techniques to analyze the adhesion of cell on molecular substrate as well as the intercellular adhesion strength. In the last years he is stably collaborating with other IIT Departments.

Selected Publications

"Cholesterol drives Aβ(1–42) interaction with lipid rafts in model membranes." Langmuir (2014) 30 (46):13934–13941

"Cellular level nanomanipulation using atomic force microscope aided with superresolution imaging." Journal of Biomedical Optics (2014) 19(10):1-9

"GRP78 clustering at the cell surface of neuronf tranduces the action of exogenous alpha-synuclein." Cell Death & Differentiation (2014) 21:1971-1983
"Resting microglia react to Abeta-42, but do not detect oligomers or oligo-induced neuronal damage." Neurobiology of Aging (2014) 35(11): 2444-2457
"Lamin B1 overexpression increases nuclear rigidity in autosomal dominant leukodystrophy fibroblasts." The FASEB Journal, (2014) 28:3906-30918

"Effects of barium titanate nanoparticles on proliferation and differentiation of rat mesenchymal stem cells" Colloids and Surfaces B (2012) 102:312-320

"Probing cytoskeleton organization of neuroblastoma cells with single cell force spectroscopy" Journal of Molecular Recognition (2012) 25:270-277

“Toxic effects of expanded ataxin-1 involve mechanical instability of the nuclear membrane” BBA Molecular Basis of Disease (2012) 1822:906-917

"Inhibiting effect of αs1-casein on Aβ1-40 aggregation” BBA General Subjects (2012) 1820:124–132

“Nanoscale structural and mechanical effects of Beta-amyloid (1-42) on polymer cushioned membranes: A combined study by neutron reflectometry and AFM force spectroscopy BBA Biomembranes (2011) 11:2646-2655

“Force spectroscopy as a tool to investigate the properties of supported lipid membranes” Microscopy Research and Technique (2010) 73:465-972

“Amyloid Fibrils Formation and Amorphous Aggregation In Concanavalin A” Biophys. Chem. (2007) 125:184-190

“Natively folded HypF-N and its early aggregates interact with phospholipid monolayers and destabilize supported lipid bilayer” Biophys. J. (2006) 91:4575-4578

“Collagen plays an active role in the aggregation of β2-microglobulin under physio-pathological conditions of dialysis-related amyloidosis” J. Biol. Chem. (2006) 281 (24):16521-16529

“Beta Amyloid is Different in Normal Aging and in Alzheimer’s Disease” J. Biol. Chem.(2005) 40:34186-34192

“Amyloid Formation from HypF-N under Conditions in wich the Protein is Initially in its Native State” J. Mol. Biol. (2005) 34:323-335

“Monitoring the Process of HypF Fibrillization and Liposome Permeabilization by Protofibrils” J. Mol. Biol. (2004) 338:943–957

 

 

 

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