Tel Aviv University, Department of Molecular Microbiology and Biotechnology
"The Physiological Significance of Protein Unfolding and Misfolding"
I received the 2002 Dan David Prize Scholarship in Biological Sciences. At this stage, I was a young faculty member. About a year and a half after I established my own laboratory. Three and a half years later, I am currently a tenured associate professor with a large laboratory of about 15 members including M.Sc. students, Ph.D. student, postdoctoral associates, and technicians. The major research interests of my laboratory are concerned with various aspects of protein unfolding, misfolding, and self-assembly.
We utilize a variety of biochemical and biophysical methodologies as well as bioinformatics and molecular biology, to study the mechanism of formation and physiological significance of non-native protein structures. The experimental systems used are diverse and the partial list includes various amyloidogenic polypeptides, tumor suppressor proteins, and bacterial toxin-antidote systems. Since the establishment of the lab, our research already provided many new insights into the process of protein unfolding and misfolding. One of our main findings is the apparent role of aromatic stacking interactions in the molecular recognition and self-assembly processes that lead to amyloid fibrils formation. That led us to novel mechanistic insights on the process of amyloid formation, identification of novel short amyloidogenic motifs (as short as pentapeptides), and development of novel methods to inhibit their formation. As amyloid formation is associated with about twenty major human disease such as Alzheimer's Disease, Parkinson's Disease, Prion Diseases (such as BSE - the "mad-cow" disease), and Type II diabetes, these results have a very significant medical importance.
The work on minimal elements had to the identification of self-assembled tubular and spherical structures in the nano-scale. We had demonstrated that aromatic entities, as simple as dipeptides, could form either nanotubes or nanospheres. We had also suggested a chemical framework for the design of new peptide derivatives that form various structures at the nano-scale. We had proven the unique chemical and physical properties of these peptide nanostructures and their usefulness in electrochemical sensors. This transformed us from Biology into Material Science studies. Indeed my Ph.D. student, Meital Reches, was awarded with the 2005 Dan David Scholarship Award in Materials Science.
The future directions in my laboratory include the development of new therapeutic agents to treat amyloid-associted diseases such as Alzheimer 's disease and Type II diabetes. We are also exploring the potential use of the nano-assemblies for their use as novel composite "Smart Materials", as vehicles for drug delivery, and as agents for novel imaging techniques.
Updated Details November 2010:
Prof. Ehud Gazit, Ph.D.
Vice President for Research and Development
Incumbent, Endowed Chair of Nano-Biology
Chairman of the Board, Ramot Ltd.
Tel Aviv University
Tel: +972-3-640-8475, Fax: +972-3-640-5448
Web (office): www.tau.ac.il/president/vp-rd-e.html
Web (Ramot Ltd.): www.ramot.org
Web (lab): www.tau.ac.il/~ehudg