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 Leblanc

Research output: Contribution to journalArticle

18 Citations (Scopus)

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 languageEnglish
Pages (from-to)6702-6704
Number of pages3
JournalChemical Communications
Volume46
Issue number36
DOIs
StatePublished - Sep 28 2010

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Synucleins
Crystal orientation
Conformations
Monolayers
Agglomeration
Intrinsically Disordered Proteins
Proteins
Water
Air

ASJC Scopus subject areas

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

Cite this

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.

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

Research output: Contribution to journalArticle

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