!!! New web site !!!
!!! New address !!!
luca.monticelli [at] inserm.fr
My main scientific interests are in the field of membrane biophysics and in the interaction between biological membranes and nano-sized particles, including both biological and synthetic macromolecules. In particular, I am interested in understanding how biological and man-made nanomaterials enter cells and perturb their functions.
Among biological macromolecules, my main interest is in protein-lipid interactions. As for synthetic nanoparticles, I am studying permeation of carbon nanoparticles (fullerenes and nanotubes) through biological membranes.
This multi-disciplinary research is coupled to the development of computational methodologies for the study of biological systems. I currently work at the development of both atomistic and coarse-grained force fields for molecular simulations.
Research and teaching experience
- 2009 – 2013: Researcher at DSIMB, INSERM UMR-S665, Paris, France.
- 2008 – 2009: Research Associate at Helsinki University of Technology (TKK), Espoo, Finland, in the group of Prof I. Vattulainen.
- 2004 – 2007: AHFMR Research Fellow at the University of Calgary, AB, Canada. Advisor: Prof. D. Peter Tieleman.
- 2003: visiting researcher at the University of Calgary, AB, Canada. Advisor: Prof. D. Peter Tieleman.
- 2002 – 2004: teaching assistant at the University Vita-Salute San Raffaele, Milan, Italy; course: « Chemistry and Propaedeutic Biochemistry ».
- 2002 – 2004: CISI Research Fellow, University of Milan, Italy. Advisors: Prof. A. Bernardi and Dr. G. Colombo.
- 1999 – 2002: PhD student at the University of Padova, Italy. Supervisor: Prof. S. Mammi.
- 1997 – 1998: research internship at DISMA, University of Milan, Italy. Supervisor: Prof. E. Ragg.
- 2002: PhD in Chemistry, University of Padova, Italy
Supervisor: Prof. S. Mammi
Thesis: Molecular dynamics simulations of the parathyroid hormone receptor system
- 1998: « Laurea » in Chemistry, University of Milan, Italy; grade 110/110
Supervisor: Prof. E. Ragg
Thesis: Conformational analysis of PrP106-126, a neurotoxic fragment of prion protein, through NMR spectroscopy