Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach.
Curr Protein Pept Sci. 2011 Feb 24;
Authors: Orcellet ML, Fernández CO
The misfolding of proteins into a toxic conformation is proposed to be at the molecular foundation of a number of neurodegenerative disorders including Alzheimer's and Parkinson's diseases. Evidence that ?-synuclein amyloidogenesis plays a causative role in the development of Parkinson's disease is furnished by a variety of genetic, neuropathological and biochemical studies. There is a major interest in understanding the structural and toxicity features of the various species populated along the aggregation pathway of this protein. The development of multidimensional nuclear magnetic resonance (NMR) spectroscopy in liquid and solid state over the last decade has significantly increased the scope of molecules that are amenable for structural studies. The aim of this review is to provide a picture of how NMR tools were used in concert to decipher the structural and dynamic properties of the intrinsically disordered protein ?-synuclein in its native, oligomeric, fibril and membrane-bound states. Understanding the structural and molecular basis behind the aggregation pathway of ?-synuclein is key to advance in the design of a therapeutic strategy.
PMID: 21348834 [PubMed - as supplied by publisher]
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Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach.
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