Generic placeholder image

Current Protein & Peptide Science


ISSN (Print): 1389-2037
ISSN (Online): 1875-5550

Structures Behind the Amyloid Aggregation of α-Synuclein: An NMR based Approach

Author(s): Maria L. Orcellet and Claudio O. Fernandez

Volume 12, Issue 3, 2011

Page: [188 - 205] Pages: 18

DOI: 10.2174/138920311795860160

Price: $65


The misfolding of proteins into a toxic conformation is proposed to be at the molecular foundation of a number of neurodegenerative disorders including Alzheimers and Parkinsons diseases. Evidence that α-synuclein amyloidogenesis plays a causative role in the development of Parkinsons 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 α- synuclein in its native, oligomeric, fibril and membrane-bound states. Understanding the structural and molecular basis behind the aggregation pathway of α-synuclein is key to advance in the design of a therapeutic strategy.

Keywords: Amyloid, intrinsically disordered proteins, NMR spectroscopy, Parkinson's disease, structural biology, Amyloid Aggregation, α-Synuclein, toxic conformation, Alzheimer's disease, Neurodegenerative Diseases, fibril morphology

Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy