Claude D. Benchimol is Senior Vice President of Research and Development of   Invitrogen Corporation, one of the world’s leading biotechnology companies. He was appointed in September 2003.

Invitrogen is a $1.2 billion life sciences company headquartered in Carlsbad, California.  Conducting business in more than 70 countries, Invitrogen provides essential life technologies for disease research, drug discovery, and commercial bioproduction.

The company’s products and services are used in nearly every major laboratory worldwide, supporting academic and government research institutions as well as pharmaceutical and biotechnology corporations.  Invitrogen employs approximately 5,000 scientists and other professionals.

Prior to joining Invitrogen, Dr. Benchimol served in a variety of executive positions at General Electric Medical Systems (GEMS).  From 2001 to 2003, Dr. Benchimol was Vice-President of Global Technology at GE’s Medical Information Technologies, which grew into a $2 billion enterprise. Prior to this role, he assumed a number of leadership positions in the development of complex diagnostic imaging instruments and innovations, like slip-ring & multi-slice CT Scanners, High Field and open MRI Scanners, Digital Mammography, and Digital Cardiology.

Dr. Benchimol received a Master’s degree in Electrical Engineering from Ecole Nationale Supérieure des Télécommunications in Paris, France.  He earned a Master’s degree in Systems Science from the University of California, Los Angeles, and he received his Doctorate in Systems Science, also from the University of California at Los Angeles.

He is a member of the French Academy of Technology, and serves on the Board of the San Diego Symphony.

Dr. Cohen is an inorganic chemist whose research is focused, in part, on the development of inhibitors of metalloproteins—proteins that contain metal ions.  His laboratory has developed strategies to use inorganic, organic, medicinal, and computational chemistry to develop new inhibitors that may be useful in a number of diseases ranging from heart disease to anthrax infections.  His studies are highly collaborative, working with biochemists, medical researchers, and others to tackle their research problems.  At the heart of their approach, is utilizing knowledge about the bioinorganic chemistry of a protein’s metal ion active site as a basis for new drug design.

Dr. Cohen’s work in this field has lead to the discovery of new inhibitors of matrix metalloproteinases (MMPs).  MMPs are digestive enzymes involved in collagen and connective tissue breakdown, and have been implicated in many pathologies including, heart disease, cancer, inflammatory disease, and stroke.  The compounds his group has developed may serve not only as therapeutics, but also as biochemical tools to better understand the role of MMPs in these different disease states.  Furthermore, in the wake of the anthrax attacks of late 2001, Dr. Cohen’s group has begun working on inhibitors of the anthrax lethal factor (LF), a metalloprotein that is key to the toxicity anthrax bacteria.

Website: http://pghosh.ucsd.edu/

Dr. Ghosh is a structural and molecular biochemist working on mechanisms used by microbial pathogens to cause infectious disease.  His laboratory is focused primarily on bacterial pathogens, which are a re-emerging threat to human health and welfare due to the increasing incidence of multidrug resistant strains.  A number of bacterial pathogens also pose threats as bioterror agents.  Dr. Ghosh is trying to understand how bacterial pathogens manipulate the behavior of human cells during infection.  This process almost always requires direct interactions between bacterial proteins, called virulence factors, and human proteins.  Dr. Ghosh first seeks to get a three-dimensional picture of both bacterial and human proteins involved in infection through X-ray crystallography.  He then applies this knowledge to the design of genetic, biochemical, and cell biological experiments aimed at understanding the mechanism of action of these molecules. 

Of primary interest to his laboratory are mechanisms used by microbial pathogens to gain entry into human cells and live as intracellular parasites.  A large variety of pathogens are known to adopt this lifestyle, and Dr. Ghosh has been dissecting the entry process in the bacterial, food-borne pathogen Listeria monocytogenes.  His laboratory is also studying mechanisms used by bacterial pathogens to inject proteins directly into human cells. 

Website: http://chem-faculty.ucsd.edu/komives/

Dr. Komives has a broad training in chemistry, pharmaceutical chemistry, and biochemistry, but lately her research has evolved to more biophysical approaches.  While in graduate school in pharmaceutical chemistry, she made it her life goal to try to understand how and why proteins interact with other proteins because nearly all drugs target protein-protein interactions, and rational design of new drugs relies on accurate understanding of the interactions they target. 

Her first project as an assistant professor at UCSD involved trying to understand how thrombomodulin modulates the activity of thrombin.  Thrombin is the last enzyme in a cascade of enzymes that cause rapid blood clot formation upon injury.  Thrombomodulin binds to thrombin and changes its activity so that it shuts down clotting.  Dr. Komives used surface plasmon resonance and NMR to show that both thrombin and thrombomodulin are dynamic molecules; they have floppy loops that move and their movement is important for rapid binding to each other.

One new approach that Dr. Komives pioneered is "MALDI-Mapping".  This experiment involves labeling the proteins in the interaction with heavy hydrogen atoms, and then watching which heavy hydrogens stay bound after the protein-protein complex is washed.  The locations of the heavy hydrogens are found by first cutting the protein in pieces and then weighing the pieces using mass spectrometry.  The MALDI-Mapping made it possible to track subtle changes in the shape of thrombin, resulting from the binding of thrombomodulin, that cause thrombin to shut down blood clotting.  Dr. Komives is taking this approach in two different directions.  On the one hand, she is trying to understand why the subtle changes in thrombin cause it to be anticoagulant.  On the other hand, she is developing MALDI-Mapping into a high through-put approach to identifying protein-protein interfaces.  She is using this to map interactions of proteins involved in Alzheimer's disease and cancer.