Protein Aggregation in Crowded Environments

The physicochemical parameters of biomolecules are the key determinants of the multitude ofprocesses that govern the normal and aberrant behavior of living systems. A particularly important aspectof such behavior is the role it plays in the self-association of proteins to form organized aggregates suchas the amyloid or amyloid-like fibrils that are associated with pathological conditions including Alzheimer’sdisease and Type II diabetes. In this study we describe quantitative quartz crystal microbalancemeasurements of the kinetics of the growth of amyloid fibrils in a range of crowded environments and inconjunction with theoretical predictions demonstrate the existence of general relationships that link thepropensities of protein molecules to aggregate with fundamental parameters that describe their specificstructures and local environments.