Meytal Landau, Ph.D. Technion – Israel Institute of Technology, Haifa
Photo: Eugene Weisberg
Meytal Landau’s first scientific interest was in the mechanisms of drug actions. She obtained her B.Sc. Pharm. (Bachelor of Pharmacy) Magna cum laude from the Hebrew University, Jerusalem, Israel. During her Master’s studies in Neurobiology at Tel-Aviv University, Israel, Meytal got familiar with neurodegenerative diseases. Her growing interests in human diseases prompt her to investigate structure-function relationships in disease-associated proteins during her Doctoral studies in Biochemistry with Prof. Nir Ben-Tal at Tel-Aviv University, Israel. Meytal’s postdoctoral studies with Prof. David Eisenberg at the University of California, Los Angeles (UCLA), USA, were focused on the biophysical characterization of amyloid proteins that are associated with Alzheimer’s and other aggregation diseases. She determined crystal structures of amyloid-like fibers complexed with small molecules, providing a model to guide structure-based design of diagnostics and inhibitors of amyloid aggregation. Meytal is now an Assistant Professor at the Technion – Israel Institute of Technology. Her lab is focused on the studies of microbial amyloids via x-ray crystallography, electron microscopy, biophysical tools, cell biology and biochemistry.
Our lab’s research objectives are to determine the structural features of peptides and proteins that form functional amyloids. These are protein aggregates, both oligomers and insoluble fibers, which serve specific functions for the organism. Mechanistic understanding of their activities has been hindered due to their partially disordered nature and the lack of high-resolution structures. To bridge this informational gap, we investigate amyloid spine segments, which were shown to recapitulate amyloid properties of their parent proteins in human amyloids involved in aggregation diseases. Importantly, such spine segments are amenable to structure determination by X-ray microcrystallography.
Our long term goal is to unravel the structure and mechanistic principles of specific amyloids, their roles in physiology and in human health and disease. Ultimately this understanding will lead to mastery over amyloid biology and offer new avenues to protein science, industry and medicine.