Seminar

A combined experimental and theoretical approach to study protein aggregation

Salvador Ventura, PhD

Protein misfolding and aggregation into amyloid structures are associated with dozens of human diseases. Recent studies have provided compelling evidence for the formation of aggregates conformationally related to those underlying such disorders in yeast and bacterial cytosols. Thus, amyloid-like aggregation seems to be an omnipresent process in both eukaryotic and prokaryotic organisms. The ease with which yeast and bacteria can be genetically and biochemically manipulated suggest that they might become useful systems for studying how and why proteins aggregate inside the cell and could provide a tractable environment to rationally model such phenomenon. This "in the cell" studies, combined with the computational analysis of the common as well as the differential structural and sequential properties of the proteins involved in human amyloid diseases might be of much help in deciphering the molecular mechanisms behind protein aggregation.