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

Published

January 5, 2017

Author(s)

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

Abstract

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.

Citation

Journal of Physical Chemistry Letters

Volume

8

Issue

1

Pub Type

Journals

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Keywords

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

Citation

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], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=921043 (Accessed April 26, 2024)