Brandon Wustman, PhD, specializes in the development of pharmacological chaperones for the treatment of diseases associated with the misfolding and mistrafficking of proteins. Dr. Wustman received his PhD in biology from Michigan Technological University in 1998. Work for this thesis focused on using a combination of microscopical, immunofluorescence and biochemical methods to study the composition, trafficking, and assembly of bioadhesives. Dr. Wustman received a doctoral fellowship from the Office of Naval Research and a postdoctoral fellowship from the Alexander Von Humboldt Society to continue his research on protein folding and trafficking at the University of Cologne in Cologne, Germany. His work at the University of Cologne focused on protein trafficking, using various molecular biology and electron microscopy methods to explore competing theories of cargo transport through the Golgi bodies, “vesicular shuttle model vs. cisternal progression.â€å In 2000, Dr. Wustman joined the chemistry department at New York University to study protein folding at the molecular level using a combination of NMR spectroscopy, MALDI/TOF and molecular modeling techniques. Since joining Amicus in 2002, he has applied a wide variety of analytical, biochemical and cell biological techniques to study the effects of pharmacological chaperones on protein folding and trafficking. His work has contributed to the development of two therapies currently in clinical trials for Fabry and Gaucher diseases. His work is also focused on developing chaperone treatments for various neurodegenerative diseases including Parkinson’s. His lab has recently identified several animal models with reduced glucocerebosidase activity (enzyme involved in Gaucher disease) that develop a Parkinson’s-like phenotype, including tremor and the accumulation of ubiquitinated alpha-synuclein. These animals are being used to study the link between Gaucher and Parkinson’s diseases and to examine the effectiveness of pharmacological chaperone treatment for the reduction alpha-synuclein accumulation in vivo.