黑料网吃瓜爆料

Research

Current Projects

Mechanisms of Amyloid Fibril Self-assembly

The main focus of our current research is on the molecular mechanisms regulating self-assembly of proteins into amyloid fibrils. Amyloid fibrils are long, nonbranching protein fibrils characterized by their cross-beta sheet architecture. These fibrils are the molecular hallmark of a multitude of human disorders that includes many neurodegenerative diseases such as Alzheimer's and Parkinson's disease, prion diseases, but also type II diabetes, light chain and lysozyme amyloidoses and, potentially, even glaucoma. At the same time, there are several examples that amyloid fibril formation is associated with functional biological activity in bacteria, yeast and even mammals. In fact, there is increasing evidence that the backbones of polypeptide chains, which are the polymers that peptides and proteins are made of, have the intrinsic propensity towards forming the intermolecular hydrogen bonds that are the structural characteristic of amyloid fibrils. Yet, many aspects of the mechanisms that induce proteins and peptides to form amyloid fibrils in vitro and in vivo remain poorly understood.