I obtained my Sc.B. degree in Biology from the Universitat Autònoma de Barcelona (UAB) in 1988. I was a Spanish Government pre-doctoral fellow in the Fundamental Biology Institute "VIcent Villar Palasí" of the UAB, where I performed my PhD thesis under the direction of Dr. Antoni Villaverde. My research interest was focused on the development of molecular tools for the optimization of the production of recombinant protein-based vaccines. From 1995 to 1998 I was a post-doctoral fellow at the Institute de Biologie Moléculaire et Cellulaire of the CNRS at Strasbourg (France) where I joined the research team leaded by Dr. Marc H.V. Van Regenmortel. My research interest was focused on the characterization of the immunogenicity and antigenicity of different recombinant proteins using BIAcore biosensors. In 1998 I joined the Department of Biology of the Faculty of Sciences at the Universitat de Girona as a post-doctoral fellow where at present I'm AssociateProfessor of Biochemistry and Molecular Biology. The research interests of the Protein Engineering Laboratory, where I work in collaboration with Dr. Marc Ribó and Dr. Maria Vilanova, are focused on protein folding and stability using ribonucleases as model enzymes as well as the development and potential use of these proteins as antitumor drugs.
Brief description of the Research lines
Proteins belonging to the pancreatic ribonuclease family constitute an excellent model to perform protein stability and folding studies because of the extensive knowledge about their structure and function available nowadays. In addition, some members of this family present some biological activities, such as antitumor, bactericidal or antiviral activity that have make them exceptional candidates as chemotherapeutics. The mechanisms underlying these abilities are not well known although are on the basis for the exploitation of these enzymes as therapeutic agents.
Our research project intends to develop basic and applied studies through the following research lines:
1. To study protein folding and oligomerization using ribonucleases as a model by investigating the role of the hydrophobic core on folding-unfolding kinetics induced by pressure and temperature and on the domain-swapping process.
2. To study the molecular basis of the cytotoxic mechanism of pancreatic ribonucleases and to design, produce and characterize new cytotoxic human pancreatic ribonuclease (HP-RNase) variants by inserting tumor-specific nuclear targeting signals and by fusing them to tumor cell-selective peptides. It will be evaluated the in vitro and in vivo antitumor capacity of these enzymes.
3. To study the mechanism of protein trans-splicing and to apply this methodology to direct the cytotoxicity of ribonucleases. It is anticipated that the information gleaned from the elemental studies will help in the design of strategies that make possible the control in vitro and in vivo the cytotoxicity of ribonucleases.