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

Chengshan Wang; Nilam Shah; Garima Thakur; Feimeng Zhou; Roger M. Leblanc

doi:10.1039/c0cc02098b

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

Chengshan Wang, Nilam Shah, Garima Thakur, Feimeng Zhou, Roger M. Leblanc

Chemistry

Research output: Contribution to journal › Article › peer-review

24 Scopus citations

Abstract

α-Synuclein, a natively unstructured protein important in the neuropathology of Parkinson's disease, was found to form a Langmuir monolayer in an α-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 α-synuclein.

Original language	English (US)
Pages (from-to)	6702-6704
Number of pages	3
Journal	Chemical Communications
Volume	46
Issue number	36
DOIs	https://doi.org/10.1039/c0cc02098b
State	Published - Sep 28 2010

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
Chemistry(all)
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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α-Synuclein in α-helical conformation at air-water interface : Implication of conformation and orientation changes during its accumulation/aggregation. / Wang, Chengshan; Shah, Nilam; Thakur, Garima; Zhou, Feimeng; Leblanc, Roger M.

In: Chemical Communications, Vol. 46, No. 36, 28.09.2010, p. 6702-6704.

Research output: Contribution to journal › Article › peer-review

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

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