Skip to main content
U.S. flag

An official website of the United States government

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you’ve safely connected to the .gov website. Share sensitive information only on official, secure websites.

Segmental Deuteration of α-Synuclein for Neutron Reflectometry on Tethered Bilayers



Zhiping Jiang, Frank Heinrich, Ryan P. McGlinchey, James M. Gruschus, Jennifer C. Lee


Neutron reflectometry (NR) is uniquely suited for studying protein interaction with phospholipid bilayers. While molecular details along the bilayer normal can be obtained on an Angstrom scale, NR cannot discern specific membrane-bound protein regions due to a lack of scattering contrast. For the first time, using native chemically ligated α-synuclein where either the first 86 or last 54 residues are deuterated, region-specific membrane interaction was identified by NR. Contrast between the two α-synuclein segments was achieved due to the neutron scattering length density difference between protium and deuterium atoms. Though neither lipid binding affinity nor interaction site was changed as judged by circular dichroism and nuclear magnetic resonance spectroscopy, respectively, protein density profiles extracted from NR revealed differences for segmentally- vs. fully-deuterated α-synuclein, highlighting the sensitivity of NR in detecting local structures on the membrane surface.
Journal of Physical Chemistry Letters


neutron reflectometry, Parkinson's disease, alpha synuclein, lipid membrane


Jiang, Z. , Heinrich, F. , McGlinchey, R. , Gruschus, J. and Lee, J. (2017), Segmental Deuteration of α-Synuclein for Neutron Reflectometry on Tethered Bilayers, Journal of Physical Chemistry Letters, [online], (Accessed April 12, 2024)
Created January 4, 2017, Updated October 12, 2021