Carmelo LA ROSA

Carmelo La Rosa, Ph.D.

Date of Birth: 27 January 1957.

Degrees: University of Catania (Italy): BA (5 years), 1984; Ph.D. in Physical-Chemistry, 1989.

Professional Experience:

1986-1988 Ph.D. Student.

1987 Grant for school of Physical-Chemistry of Biological Systems.

1988 Grant of Physics of Liquid Crystals.

1989 Ph.D. degree.

1990-1996 Research Fellow in Chemistry, University of Catania.

1990 Member of organizer committee III Meeting Italia-URSS ON PHYSICS OF LIQUID CRYSTALS AND LANGMUIR-BLODGETT FILMS.

1991 Invited researcher, Dipartimento di Chimica, Università di Napoli Federico II.

1997 Assistant Professor of Physical-Chemistry

1998 Invited lecture “International Symposium: Protein Structure, Stability and Folding. Fundamental and Medical Aspects” in Moscow (Russia).

1998 Visiting researcher, Chemistry Department, ProtMet Group (Prof. G. Canters) Gorleaus Laboratoria, University of Leiden, The Nederland.

2004 -Member of Resource and Support Management of Department of Chemical Sciences, Department of Chemical Sciences, University of Catania.

2004 –Member of University of Catania, Academic Founding Committee for Chemistry.

2008- Member of organizer and scientific committee 8-th National Meeting of the Italian Liquid Crystal Society.

2011 - Head of Lyotropic Liquid Crystals Laboratory.

2012- Editorial Board Member of Word Journal of Diabetes.

2012 - Grant application evaluator of Natural Sciences and Engineering Research Council of Canada (NSERC).

2012 - Grant application evaluator of Italian Super Computing Resource Allocation (CINECA).

2013 – Visiting Professor “Sensing Amyloid Proteins: a project” King’s College London, London (GB).

2015 - Grant application evaluator of French National Research Agency (ANR).

2016 - Grant application evaluator of Ministry of National Education and Scientific Research of Romania.

2016 – Grant application evaluator Italian PRIN 2015.

2016 – Evaluator peer-review/ Italian research quality VQR 2011-2014.

2017 – Chairs: Carmelo La Rosa (University of Catania, Italy), Ayyalusamy Ramamoorthy (University of Michigan, USA) and Giuseppe Melacini (McMaster University, Canada): International Symposium on Protein Misfolding Diseases, July 31- August 3, 2017, University of Catania, Italy.

2019 – Editorial board member of Molecules Journal (MDPI), Physical-Chemistry section.

2021 - QS Word Academic Rankings evaluator.

2021 – Chairs: Carmelo La Rosa (University of Catania), Danilo Milardi (CNR), Ayyalusamy Ramamoorthy (University of Michigan, USA): International Symposium on Pathomechanism of Amyloid Diseases, September 15-17, 2021 University of Catania, Italy.

• ORCID: 0000-0002-7123-5347
• CINECA IRIS Institutional Research Information System: link

Protein Folding-Misfolding and Aggregation. Folding is a process by which a protein passes from random coil state to a well-defined and unique three dimensional structure (native state). Protein folding reaction have a finite tendency either to misfold, or to fail to maintain their correctly folded. Folding-unfolding reactions are in competition and under some circumstances one of the two prevails. If unfolding reaction prevails and escape the cellular quality-control mechanism some proteins aggregate and form pseudo-ordered aggregate called fibrils. Proteins with this special features are called amyloidogenic proteins and amyloid the formed aggregate. This conditions in living systems lead to pathological state. The most famous are Type II diabetes mellitus, Alzheimer, Parkinson, Transmissible Spongiform Encephalopathies, lateral amyotrophic sclerosis and so on. In our laboratory we look for chemical-physical parameters that govern the aggregation processes of amyloidogenic proteins. In particular, we investigate the structures and dynamics of pre-fibrillar state (oligomeric state), since amyloid oligomers have emerged as toxic species in amyloid diseases. Also, molecules able to disfavor aggregation process are studied.

Lyotropic Liquid crystals – model membrane. Cellular membranes play an important role in the survival of the cell itself. They separate a disordered environment, the extracellular space, from a crowded but highly ordered environment like intracellular space. Cellular membranes have a very complex structure. They have an asymmetric composition containing many types of phospholipids, proteins and cholesterol. The complexity of biological membranes has motivated the development of a variety of simpler model systems whose size, geometry, and composition that can be designed with great precision. Moreover, in the past was suggested the crucial role playing membrane in the abnormal aggregation and toxicity of amyloidogenic proteins. In our laboratory, we investigate the interaction of complex model membrane with amyloidogenic proteins. Also, the influence of some metal ions such as calcium and zinc on amyloid formation are investigated.

Methods. Our study are conducted using both experimental and computational techniques. Experiments are conducted using Circular Dichroism, Differential Scanning Calorimetry, Fluorescence, Optical Density, Atomic Force Microscopy, Dynamic Light Scattering. Computer simulations done mainly by GROMAS package software using All Atom, United Atom and Coarse Grained Force Field.