α-Synuclein Sterically Stabilizes Spherical Nanoparticle-Supported Lipid Bilayers

Chung, Peter J.; Zhang, Qingteng; Hwang, Hyeondo Luke; Leong, Alessandra; Maj, Piotr; Szczygiel, Robert; Dufresne, Eric M.; Narayanan, Suresh; Adams, Erin J.; Lee, Ka Yee C.

doi:10.1021/acsabm.8b00774

Title: α-Synuclein Sterically Stabilizes Spherical Nanoparticle-Supported Lipid Bilayers

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Abstract

While it is generally accepted that neuronal protein α-synuclein binds to highly curved and highly charged lipid membranes, its biological function beyond binding remains unknown despite its fundamental link to Parkinson’s disease. Herein, we utilize spherical nanoparticle lipid bilayers (SSLBs) to recapitulate the charge and curvature limit of membrane organelles with which α-synuclein associates and probe how α-synuclein affects SSLB structure and dynamics as a proxy for interorganelle interactions. Furthermore, small-angle X-ray scattering and X-ray photon correlation spectroscopy reveal our SSLBs form aggregates that are clearly broken up by the addition of α-synuclein, a clear indication that α-synuclein confers steric stabilization to membrane surfaces.

Authors:

^[1];

^[2]; Hwang, Hyeondo Luke ^[1]; Leong, Alessandra ^[1];

^[3];

^[2]; Narayanan, Suresh ^[2]; Adams, Erin J. ^[1];

^[1]

The Univ. of Chicago, Chicago, IL (United States)
Argonne National Lab. (ANL), Lemont, IL (United States)
AGH Univ. of Science and Technology, Kraków (Poland)

Publication Date:: Thu Feb 28 00:00:00 EST 2019

Research Org.:: Argonne National Lab. (ANL), Argonne, IL (United States)

Sponsoring Org.:: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Science Foundation (NSF)

OSTI Identifier:: 1559046

Grant/Contract Number:: AC02-06CH11357

Resource Type:: Accepted Manuscript

Journal Name:: ACS Applied Bio Materials

Additional Journal Information:: Journal Volume: 2; Journal Issue: 4; Journal ID: ISSN 2576-6422

Publisher:: ACS Publications

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; spherical nanoparticle-supported lipid bilayers; synchrotron X-ray photon correlation spectroscopy (XPCS); synchrotron small-angle X-ray scattering (SAXS); α-synuclein

Citation Formats


                    Chung, Peter J., Zhang, Qingteng, Hwang, Hyeondo Luke, Leong, Alessandra, Maj, Piotr, Szczygiel, Robert, Dufresne, Eric M., Narayanan, Suresh, Adams, Erin J., and Lee, Ka Yee C. α-Synuclein Sterically Stabilizes Spherical Nanoparticle-Supported Lipid Bilayers.  United States: N. p., 2019. 
Web.  doi:10.1021/acsabm.8b00774.

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                    Chung, Peter J., Zhang, Qingteng, Hwang, Hyeondo Luke, Leong, Alessandra, Maj, Piotr, Szczygiel, Robert, Dufresne, Eric M., Narayanan, Suresh, Adams, Erin J., & Lee, Ka Yee C. α-Synuclein Sterically Stabilizes Spherical Nanoparticle-Supported Lipid Bilayers.  United States.  https://doi.org/10.1021/acsabm.8b00774

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                    Chung, Peter J., Zhang, Qingteng, Hwang, Hyeondo Luke, Leong, Alessandra, Maj, Piotr, Szczygiel, Robert, Dufresne, Eric M., Narayanan, Suresh, Adams, Erin J., and Lee, Ka Yee C. Thu .  
"α-Synuclein Sterically Stabilizes Spherical Nanoparticle-Supported Lipid Bilayers".  United States.  https://doi.org/10.1021/acsabm.8b00774.  https://www.osti.gov/servlets/purl/1559046.

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@article{osti_1559046,

  title        = {α-Synuclein Sterically Stabilizes Spherical Nanoparticle-Supported Lipid Bilayers},

  author       = {Chung, Peter J. and Zhang, Qingteng and Hwang, Hyeondo Luke and Leong, Alessandra and Maj, Piotr and Szczygiel, Robert and Dufresne, Eric M. and Narayanan, Suresh and Adams, Erin J. and Lee, Ka Yee C.},

  abstractNote = {While it is generally accepted that neuronal protein α-synuclein binds to highly curved and highly charged lipid membranes, its biological function beyond binding remains unknown despite its fundamental link to Parkinson’s disease. Herein, we utilize spherical nanoparticle lipid bilayers (SSLBs) to recapitulate the charge and curvature limit of membrane organelles with which α-synuclein associates and probe how α-synuclein affects SSLB structure and dynamics as a proxy for interorganelle interactions. Furthermore, small-angle X-ray scattering and X-ray photon correlation spectroscopy reveal our SSLBs form aggregates that are clearly broken up by the addition of α-synuclein, a clear indication that α-synuclein confers steric stabilization to membrane surfaces.},

  doi          = {10.1021/acsabm.8b00774},

  journal      = {ACS Applied Bio Materials},

  number       = 4,

  volume       = 2,

  place        = {United States},

  year         = {Thu Feb 28 00:00:00 EST 2019},

  month        = {Thu Feb 28 00:00:00 EST 2019}

}

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