Dorothy and Patrick E. Gorman Professor of Biological Ultrastructure

Born in Padova, Italy, Lia Addadi obtained her B.Sc. and M.Sc. degrees in Organic Chemistry at the Università degli Studi di Padova, and a Ph.D. in Structural Chemistry from the Weizmann Institute of Science in 1979. Her postdoctoral studies were carried out at Harvard University. In 1982, Prof. Addadi returned to the Weizmann Institute, joining the staff of the Department of Structural Chemistry (now the Department of Structural Biology, which she headed from 1994-2001). She was appointed Associate Professor in 1988, Full Professor in 1993, and Dean of the Faculty of Chemistry 2001-2004.

A recipient of numerous prizes and honors, she was awarded the Prelog Medal in Stereochemistry in 1998 by the ETH of Zurich, and is the 2006 recipient of the Kolthof prize of the Technion-Israel Instute of Technology Prof. Addadi is the incumbent of the Dorothy and Patrick E. Gorman Professorial Chair of Biological Ultrastructure.

Prof. Addadi pursues a broad range of research interests that relate to crystals. She studies mineralization in biological systems, with a particular interest in crystallizations that have either a physiological function or a pathological outcome in a wide variety of organisms, including humans. Her work incorporates research that has a bearing on osteoporosis, atherosclerosis, amyloid formation and some types of arthritis. Her research on biomineralization, undertaken in conjunction with departmental colleague Prof. Steve Weiner, elucidates the strategies evolved by nature to produce composite materials, which may lead to inspiration for new mechanical, optical or electronic devices.

Prof. Addadi also collaborates with Prof. Benny Geiger (Molecular Cell Biology) in researching recognition in cell adhesion, and in studies of the mechanism of bone resorption (dissolution) by specialized cells called osteoclasts.

Antibody Recognition of Cholesterol-rich Structures: Following on Dorothy Hodgkin's Path
The interactions between proteins and crystal surfaces range from totally non-specific physical adsorption of the macromolecule on the surface to the most highly specific recognition. Among proteins, antibodies are the tools that nature evolved to recognize foreign invaders, by virtue of their complementarity to the surface of the invader.

When introduced into an organism, crystals do not expose to the environment the whole chemical entity of their component molecules but rather appear as highly structured repetitive macromolecular substrates. An antibody that recognizes a crystal face can thus bear in its binding site a structured imprint of a number of molecular moieties exposed on the crystal surface.

Within the last several years, investigations based on this concept led to the isolation and characterization of a battery of monoclonal antibodies that recognize certain crystalline organizations with high specificity. Among those, we are presently developing and investigating antibodies which selectively label organized cholesterol-associated cell membrane domains. These studies may contribute to the understanding of the structure of lipid rafts and of the formation of atherosclerotic plaques.