Self-assembly of short aromatic peptides: from amyloid disease to nanotechnology
My lab is interested in Molecular Structure and Self-Assembly at the Nano-Scale.
The central dogma in the study of protein folding suggests that the thermodynamically-favorable state of proteins under physiological conditions is their folded one. However, there are number of cases in which the favorable states of proteins are rather unfolded, partially folded (e.g., "molten globular"), or misfolded (e.g., nonspecific aggregates or amyloid fibrils). These observations lead to much interest in the significance and mechanism of formation of such unfolded, misfolded or partially folded structures in physiological as well as pathological conditions.
In our lab we utilize a variety of biochemical, biophysical and molecular biology methodologies to study the mechanism and significance of protein unfolding and misfolding. The experimental systems used are diverse and the partial list includes several bacterial toxin-antidote systems, type II diabetes-related amyloidogenic proteins and peptides, and the VHL tumor suppressor protein. We also study the mechanism of non-specific aggregation of generic unrelated proteins. Another line of research is directed toward the elucidation of the mechanism of action of chemical chaperons and their effect on folding, aggregation and amyloid formation.
For a more details on specific lab activities, please read the full research description.