UPDATE: A recent independent study by the Petsko-Ringe and Pochapsky laboratories at Brandeis University in Waltham, MA, has confirmed the native tetrameric structure of alpha-synuclein proposed by Selkoe and colleagues.

In a recent study that could radically change our understanding of the pathophysiology of Parkinson’s disease, principal investigator Dennis J. Selkoe at Brigham and Women’s Hospital and Harvard Medical School discovered that the overall three-dimensional structure of alpha-synuclein, a protein that abnormally aggregates as Lewy bodies in the brains of Parkinson’s patients, has likely been mischaracterized. Prior to this study, scientists had thought that alpha-synuclein in healthy cells is arranged as a randomly coiled chain with no apparent orderly structure. Selkoe’s lab, however, has shown otherwise in their study published online August 14 in Nature.

Aside from being structurally disordered, alpha-synuclein had been previously assumed to functionally exist as a monomer. In contrast, the new study reveals that the protein is organized in a complex of four individual alpha-synuclein units, each with alpha-helical folding.

So what's the significance of this finding?

The researchers hypothesize that the development and/or progression of Parkinson's disease begins with destabilization of the alpha-synuclein tetramer. The monomeric proteins then misfold and aggregate into Lewy bodies which accumulate with advancement of the disease. Accordingly, this finding could provide avenues to new therapeutic approaches for the treatment or prevention of Parkinson’s.

Read more from the official release by Harvard Medical School.
Full original research article available here.