From the beginning until present
I obtained my Sc.B. degree in Chemistry from the Universitat Autònoma de Barcelona (UAB). I was a Spanish Government pre-doctoral fellow in the Biochemistry and Molecular Biology Department of the UAB. There I worked with Prof. F. X. Avilés to elucidate the activation mechanism of pancreatic zymogens. I earned my Ph. D. degree in Biochemistry in 1987. I was a post-doctoral fellow at the Institut de Biologia Fonamental (UAB) where I worked with Prof. C. M. Cuchillo who introduced me in the field of ribonucleases. In 1990 I joined the Department of Biology of the Faculty of Sciences at the Universitat de Girona where at present I'm Full Professor of Biochemistry and Molecular Biology. The research interests of the Protein Engineering Laboratory, where I work in collaboration with Dr. Marc Ribó and Dr. Antoni Benito, 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 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.
2. To study the molecular basis of the cytotoxic mechanism of the antitumor viral protein named apoptin.
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.