Current Research

Parkinson’s Disease

Parkinson’s Disease is the second most common neurodegenerative condition in the US behind Alzheimer’s Disease. It is characterized by loss of motor control resulting from damage to dopamine-producing neurons. We are studying the molecule responsible for this cellular damage, a protein called alpha-synuclein. The hallmark of Parkinson’s Disease is the presence of intracellular fibrous aggregates made up of alpha-synuclein. It is widely believed that these alpha-synuclein aggregates play a causal role in damaging the dopamine-producing neurons in which they are found.

Parkinson’s Disease is characterized by loss of motor control resulting from damage to dopamine-producing neurons.  We are studying the molecule which may be responsible for this neuronal damage, a protein called alpha-synuclein.  The hallmark of Parkinson’s disease is the presence of intracellular fibrous aggregates made up of alpha-synuclein.  It is widely believed that these alpha-synuclein aggregates play a causal role in damaging the dopamine-producing neurons in which they are found(5).

5. Uversky VN. Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation.  Journal of Neurochemistry, 2007, 103, 17-37.

Single Molecule Force Spectroscopy for Studying Alpha-Synuclein

Unlike most proteins in the human body, alpha-synuclein does not fold into a fixed three-dimensional structure.  Alpha-synuclein belongs to a class of proteins called “intrinsically unstructured proteins,” which are capable of folding into a variety of shapes.  In Parkinson’s Disease, alpha-synuclein molecules misfold into certain shapes that are prone to aggregation.  We use single molecule force spectroscopy to study how individual alpha-synuclein molecules respond to mechanical force, which sheds light on how susceptible they are to conformational changes.  Such studies will pave the way for new molecular therapeutics that could prevent the aggregation of alpha-synuclein before it starts.

Article posted on July 17, 2009