Membrane-Protein-Hydration Interaction of α-Synuclein with Anionic Vesicles Probed via Angle-Resolved Second-Harmonic Scattering
Journal article, 2019

Amyloid formation of the protein α-synuclein promotes neurodegeneration in Parkinson's disease. The normal function of α-synuclein includes synaptic vesicle transport and fusion, and the protein binds strongly to negatively charged vesicles in vitro. Here, we demonstrate that nonresonant angle-resolved second-harmonic scattering detects α-synuclein binding to liposomes through changes in water orientational correlations and can thus be used as a high-accuracy and high-throughput label-free probe of protein-liposome interactions. The obtained results support a binding model in which the N-terminus of α-synuclein adopts an α-helical conformation that lies flat on the vesicle surface while the negatively charged C-terminus remains in solution.

Author

Jan Dedic

Ecole Polytechnique Federale De Lausanne

Sandra Rocha

Chalmers, Biology and Biological Engineering, Chemical Biology

Halil I. Okur

Ecole Polytechnique Federale De Lausanne

Pernilla Wittung Stafshede

Chalmers, Biology and Biological Engineering, Chemical Biology

Sylvie Roke

Ecole Polytechnique Federale De Lausanne

Journal of Physical Chemistry B

1520-6106 (ISSN) 1520-5207 (eISSN)

Vol. 123 5 1044-1049

Subject Categories

Physical Chemistry

Biochemistry and Molecular Biology

Biophysics

DOI

10.1021/acs.jpcb.8b11096

PubMed

30625272

More information

Latest update

11/8/2019