4.7 Article

alpha-Synuclein in alpha-helical conformation at air-water interface: implication of conformation and orientation changes during its accumulation/aggregation

Journal

CHEMICAL COMMUNICATIONS
Volume 46, Issue 36, Pages 6702-6704

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c0cc02098b

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Funding

  1. NINDS [SC1NS070155-01]
  2. NIH [P20-MD001824-01]
  3. Natural Science Foundation [CBET-0944290]
  4. NATIONAL CENTER ON MINORITY HEALTH AND HEALTH DISPARITIES [P20MD001824] Funding Source: NIH RePORTER
  5. NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [SC1NS070155] Funding Source: NIH RePORTER

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alpha-Synuclein, a natively unstructured protein important in the neuropathology of Parkinson's disease, was found to form a Langmuir monolayer in an alpha-helical conformation with its helical axis parallel to the air-water interface. This study sheds light on the role of vesicles in neuronal cells in the accumulation/aggregation of alpha-synuclein.

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