Bruno Samorì

 

Office Address: Dipartimento di Biochimica “G. Moruzzi”

Via Irnerio 48 40126 Bologna (Italy)

 

e-mail: samori@alma.unibo.it

 

Curriculum Vitae

 

Bruno Samorì
Education:
1968  Laurea in Industrial Chemistry at the University of Bologna.

Training and Fellowship Appointments:
1974,1975 visiting scientist, Department of Chemistry of the King's College, London;
1982, 1983 visiting scientist, Department of Chemistry of  the University of California Berkeley

Faculty Appointments
1972-1980 Research Assistant, University of Bologna,
1980-1990 Associate Professor of Organic Chemistry, University of Bologna
1990-1995  Professor of Organic Chemistry, University of Cosenza,
2012-present “Professore Alma Mater”, University of Bologna

Memberships in Professional and Scientific Societies:
President of Italian Society of Microscopy (2001-2003),
Member (1993-2002) and also President (1999) of the Advisory Board of the Division of the Biological Systems Chemistry of the Italian Chemical Society.

Peer Review Committees (selected)
Editorial Advisory Board of ChemBioChem ( Wiley-VCH) from the foundation to 2011;
Editorial Board of Open Journal of Applied Sciences from 2012 ;
Editorial Board of Frontiers in Biophysics from 2013

Referee for  Wiley-VCH journals: Angewandte Chemie Int. Edit.; Advanced Materials ; Small; ChemBioChem; Chemistry A European Journal 
For Royal Chemical Society journal: Chemical Comunications 
For American Chemical Society: Journal of the American Chemical Society; Nano Letters; Langmuir 
Biophysical Journal 
Evaluation Committee of Swiss National Science Foundation (SNSF).

Current main research interest
Nanoscience of proteins . Understanding the inner working of proteins is one of the major frontiers in biology. Proteins fold, perform their functions, eventually miss-fold and aggregate through structural changes. We investigate these mechanical processes using the atomic force microscope in its single-molecule force spectroscopy mode examining the response of proteins to applied external forces. In particular we employed for the first time this technique to study naturally disordered proteins, detecting partially structured intermediates that favour the formation of amyloid fibrils responsible of diseases such that Parkinson's and Creutzfeld-Jacob's. Controlling these intermediates is crucial to prevent the formation of amyloid fibrils and can lead to new approaches and strategies in drug design. Supported by a Human Frontier Science Program grant the main focus of our activity is now on the molecular basis of the infectivity of the prion proteins associated to the Creutzfeld-Jacob's disease. The same methodology is presently applied to the study of the mechanism by which the, so called, osmolytes protect/hinder protein folding. They are small organic molecues that are produced or taken from the environment by numerous organisms and tissues to maintain cellular function in stressed conditions (e.g. dehydration, high T and/or P, high salt content).

Former research interests
1) DNA-protein indirect - recognition: mapping the modulation of local DNA chain curvature and
flexibility by the sequence.
2) DNA-based nanotechnologies towards the realization of nanomotors and switches.
3) DNA-based liquid crystals ( during the eighties and middle nineties)

 

Grant Awards (among the most recent ones):
Human Frontier Science Program (Awards - RGP2011; 2011-2014);
European Commission -FP6 Integrated Project “Dynamics”;
European Science Foundation Eurocores. Project: Bio-nanostructuring for molecular electronics (BIONICS: 2004–2007);
European Commission -FP6 –STREP Project “Nucleic acid based nanostructures (NUCAN: 2005–2007 );
MURST FIRB Nanobiotecnologie: Progetto “Nanosized Cancer Polymarker Biochip” (2005-2010) ,
MURST FIRB Progetto “Nanobiotecnologie per dispositivi e sensori innovativi” (2005-2008) ;
 MURST FIRB Progetto Metodologie e tecnologie innovative per la farmaceutica (2005-2008) ;
 MURST FISR Progetto “Nanotecnologie e Microsistemi” (2005-2008) ;

Invited speaker at International Meetings (selected among the most recent)
The 15th European Microscopy Congress, Manchester Central, United Kingdom, 16th - 21st September 2012;  AFM BioMed Conference, Paris, France 2011; Biophysics School “Molecular Mechanisms of Neurodegeneration” Venice  January 25th -29th, 2010;Workshop "Thermodinamically Unstable Proteins: Chance or Necessity” at  International Center for Theoretical Physics (ICTP) in Grignano (Trieste), on December 14-16, 2009; Summer School "Physics And Chemistry In Nanobiotechnology" (Jesi 1-4 September 2009); Albany: The 16th conversation (Structural Biology) June 16-20 2009; Single molecule Biophysics (Aspen Center for Physics, February 4-9, 2007); Advanced Optical Microscopy Methods in Biophysics (Venice, Jan. 29.- Febr.2, 2007); 5th Brazilian Materials Research Society Meeting, (Florianopolis, Oct. 8-12, 2006), Biophys 06: Back to the Nature,Theoretical Physics efforts real world challenges (Arcidosso Italy, September 6-8, 2006); Symposium "DNA-Based Nanoscale Integration" (Jena, May 18-20, 2006), From Solid state to Biophysics III” (Dubrovnik, Croatia  June 24 –July 1 2006)
Most recent publications (selected)

Brucale M1, Schuler B, Samorì B.
Single-Molecule Studies of Intrinsically Disordered Proteins.
Chem Rev. 2014 Jan 17. [dx.doi.org/10.1021/cr400297g]

 Brucale M, Tessari I, Bubacco L, Samorì B.
Single-molecule force spectroscopy of chimeric polyprotein constructs containing intrinsically disordered domains.
Methods Mol Biol. 2012;896:47-56. doi: 10.1007/978-1-4614-3704-8_3.

Micaela Pivato, Giorgia De Franceschi, Laura Tosatto, Erica Frare, Kumar Dhruv, Daniel Aioanei, Marco Brucale, Isabella Tessari, Marco Bisaglia, Bruno Samori, Patrizia Polverino de Laureto, Luigi Bubacco:
“Covalent a-synuclein dimers: chemico-physical and aggregation properties”
PLoS One. 2012;7(12):e50027. doi: 10.1371/journal.pone.0050027. Epub 2012 Dec 13.

Daniel Aioanei, Bruno Samorì, Marco Brucale
Worm-like Ising model for protein mechanical unfolding under the effect of osmolytes”
BIOPHYS. J, 2012, doi: 10.1016/j.bpj.2011.12.007

Daniel Aioanei, Shanshan Lv, Isabella Tessari, Aldo Rampioni, Luigi Bubacco, Hongbin Li, Bruno Samorì;, Marco Brucale,
“Single Molecule Level Proof of the Osmophobic Effect,”
 ANGEWANDTE CHEM INT. ED. (DOI: 10.1002/anie.200)  2011, 50 (19) 4394–4397

Daniel Aioanei, Isabella Tessari, Luigi Bubacco, Bruno Samorì8;, Marco Brucale,
“Observing the osmophobic effect in action at the single molecule level”
PROTEINS: 2011; 79:2214– 2223.

Marco Brucale, Massimo Sandal, Selena Di Maio, Aldo Rampioni, Isabella Tessari, Laura Tosatto, Marco Bisaglia, Luigi Bubacco, and Bruno Samorì,
“Pathogenic mutations shift the equilibria of alpha- synuclein single molecules towards structured conformers “CHEMBIOCHEM 2009, 10, 176-183

Massimo Sandal, Francesco Valle, Isabella Tessari, Stefano Mammi, Elisabetta Bergantino, Francesco Musiani, Marco Brucale, Luigi Bubacco, and Bruno Samori; -
“Conformational Equilibria in Monomeric alpha-Synuclein at the Single Molecule Level”
 PLOS BIOLOGY 2008, 6, 999-1008

Tessari, M. Bisaglia, F. Valle, B. SamorÏ, E. Bergantino, S. Mammi and L. Bubacco,
“The reaction of alpha-synuclein with tyrosinase: possible implications for Parkinson disease”
JOURNAL OF BIOLOGICAL CHEMISTRY 2008, 24, 16808-16817

B. Samorì
Plenty of room for biology at the bottom.
ANGEWANDTE CHEM INT. ED. 2008, 47, 236

Francesco Valle, Giampaolo Zuccheri, Anna Bergia, Lee Ayres, Alan†E. Rowan, Roeland†J.†M. Nolte, Bruno SamorÏ
A Polymeric Molecular "Handle" for Multiple AFM-Based Single-Molecule Force Measurements
Angewandte Chemie Int. Ed. 2008, 47, 2431-2434

 

Karl-Heinz Altmann, Johannes Buchner, Horst Kessler, FranÅois Diederich, Bernhard Kr utler, Stephen Lippard, Rob Liskamp, Klaus M ller, Elizabeth M. Nolan, Bruno Samorì, Gisbert Schneider, Stuart L. Schreiber, Harald Schwalbe, Claudio Toniolo, Constant A. A. van Boeckel, Herbert Waldmann, and Christopher T. Walsh
The State of the Art of Chemical Biology
ChemBioChem 2009, 10, 16-29

G. Zuccheri & B. Samorì (Ed.s)
DNA Nanotechnology: Methods and Protocols
Humana Press, Springer Science LLC 2011