Issue 36, 2010
From the journal:

Chemical Communications

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

Chengshan Wang,a   Nilam Shah,a   Garima Thakur,b   Feimeng Zhou*a  and  Roger M. Leblanc*b  

* Corresponding authors

a 5151 State University Drive, California State University, Los Angeles, Los Angeles, USA
E-mail: fzhou@calstatela.edu
Fax: +1 323-343-6490
Tel: +1 323-343-2390

b 1301 Memorial Drive, Department of Chemistry, University of Miami, Coral Gables, USA
E-mail: rml@miami.edu
Fax: +1 305-284-4571
Tel: +1 305-284-2194

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.

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

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Article information

DOI
https://doi.org/10.1039/C0CC02098B
Article type
Communication
Submitted
25 Jun 2010
Accepted
26 Jul 2010
First published
16 Aug 2010

Chem. Commun., 2010,46, 6702-6704

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

C. Wang, N. Shah, G. Thakur, F. Zhou and R. M. Leblanc, Chem. Commun., 2010, 46, 6702 DOI: 10.1039/C0CC02098B

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