Neutron Scattering Studies of the Interplay of Amyloid β Peptide(1–40) and An Anionic Lipid 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol
Abstract
The interaction between lipid bilayers and Amyloid β peptide (Aβ) plays a critical role in proliferation of Alzheimer’s disease (AD). AD is expected to affect one in every 85 humans by 2050, and therefore, deciphering the interplay of Aβ and lipid bilayers at the molecular level is of profound importance. In this work, we applied an array of neutron scattering methods to study the structure and dynamics of Aβ(1–40) interacting 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol (DMPG) bilayers. In the structural investigations of lipid bilayer’s response to Aβ binding, Small Angle Neutron Scattering and Neutron Membrane Diffraction revealed that the Aβ anchors firmly to the highly charged DMPG bilayers in the interfacial region between water and hydrocarbon chain, and it doesn’t penetrate deeply into the bilayer. This association mode is substantiated by the dynamics studies with high resolution Quasi-Elastic Neutron Scattering experiments, showing that the addition of Aβ mainly affects the slower lateral motion of lipid molecules, especially in the fluid phase, but not the faster internal motion. The results revealed that Aβ associates with the highly charged membrane in surface with limited impact on the structure, but the altered membrane dynamics could have more influence on other membrane processes.
- Authors:
-
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Biology and Soft Matter Division
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Chemical and Engineering Material Division
- Publication Date:
- Research Org.:
- Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). High Flux Isotope Reactor (HFIR); Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS); Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). Center for Structural Molecular Biology (CSMB)
- Sponsoring Org.:
- USDOE Laboratory Directed Research and Development (LDRD) Program; USDOE Office of Science (SC), Biological and Environmental Research (BER); USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1295105
- Grant/Contract Number:
- AC05-00OR22725; FWP ERKP291; LOIS-6436
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Scientific Reports
- Additional Journal Information:
- Journal Volume: 6; Journal Issue: 30983; Journal ID: ISSN 2045-2322
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; Amyloid Beta; Alzheimer s disease; Lipid-peptide Interactions
Citation Formats
Rai, Durgesh K., Sharma, Veerendra K., Anunciado, Divina, O’Neill, Hugh, Mamontov, Eugene, Urban, Volker, Heller, William T., and Qian, Shuo. Neutron Scattering Studies of the Interplay of Amyloid β Peptide(1–40) and An Anionic Lipid 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol. United States: N. p., 2016.
Web. doi:10.1038/srep30983.
Rai, Durgesh K., Sharma, Veerendra K., Anunciado, Divina, O’Neill, Hugh, Mamontov, Eugene, Urban, Volker, Heller, William T., & Qian, Shuo. Neutron Scattering Studies of the Interplay of Amyloid β Peptide(1–40) and An Anionic Lipid 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol. United States. https://doi.org/10.1038/srep30983
Rai, Durgesh K., Sharma, Veerendra K., Anunciado, Divina, O’Neill, Hugh, Mamontov, Eugene, Urban, Volker, Heller, William T., and Qian, Shuo. Tue .
"Neutron Scattering Studies of the Interplay of Amyloid β Peptide(1–40) and An Anionic Lipid 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol". United States. https://doi.org/10.1038/srep30983. https://www.osti.gov/servlets/purl/1295105.
@article{osti_1295105,
title = {Neutron Scattering Studies of the Interplay of Amyloid β Peptide(1–40) and An Anionic Lipid 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol},
author = {Rai, Durgesh K. and Sharma, Veerendra K. and Anunciado, Divina and O’Neill, Hugh and Mamontov, Eugene and Urban, Volker and Heller, William T. and Qian, Shuo},
abstractNote = {The interaction between lipid bilayers and Amyloid β peptide (Aβ) plays a critical role in proliferation of Alzheimer’s disease (AD). AD is expected to affect one in every 85 humans by 2050, and therefore, deciphering the interplay of Aβ and lipid bilayers at the molecular level is of profound importance. In this work, we applied an array of neutron scattering methods to study the structure and dynamics of Aβ(1–40) interacting 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol (DMPG) bilayers. In the structural investigations of lipid bilayer’s response to Aβ binding, Small Angle Neutron Scattering and Neutron Membrane Diffraction revealed that the Aβ anchors firmly to the highly charged DMPG bilayers in the interfacial region between water and hydrocarbon chain, and it doesn’t penetrate deeply into the bilayer. This association mode is substantiated by the dynamics studies with high resolution Quasi-Elastic Neutron Scattering experiments, showing that the addition of Aβ mainly affects the slower lateral motion of lipid molecules, especially in the fluid phase, but not the faster internal motion. The results revealed that Aβ associates with the highly charged membrane in surface with limited impact on the structure, but the altered membrane dynamics could have more influence on other membrane processes.},
doi = {10.1038/srep30983},
journal = {Scientific Reports},
number = 30983,
volume = 6,
place = {United States},
year = {Tue Aug 09 00:00:00 EDT 2016},
month = {Tue Aug 09 00:00:00 EDT 2016}
}
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Amyloid, the presenilins and Alzheimer's disease
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Peptides in lipid bilayers: structural and thermodynamic basis for partitioning and folding
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Phase transitions and fluidity characteristics of lipids and cell membranes
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Nanoscopic Dynamics of Phospholipid in Unilamellar Vesicles: Effect of Gel to Fluid Phase Transition
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Partially Folded Intermediates as Critical Precursors of Light Chain Amyloid Fibrils and Amorphous Aggregates †
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Two States of Cyclic Antimicrobial Peptide RTD-1 in Lipid Bilayers
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Interaction of Alzheimer β-Amyloid Peptide(1−40) with Lipid Membranes †
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Location of .beta.-sheet-forming sequences in amyloid proteins by FTIR
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Peptide-Induced Asymmetric Distribution of Charged Lipids in a Vesicle Bilayer Revealed by Small-Angle Neutron Scattering
journal, August 2011
- Qian, Shuo; Heller, William T.
- The Journal of Physical Chemistry B, Vol. 115, Issue 32
Amyloid Aggregation: Role of Biological Membranes and the Aggregate–Membrane System
journal, January 2014
- Bucciantini, Monica; Rigacci, Stefania; Stefani, Massimo
- The Journal of Physical Chemistry Letters, Vol. 5, Issue 3
Diffraction Techniques for Nonlamellar Phases of Phospholipids
journal, October 2004
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- Langmuir, Vol. 20, Issue 21
Effects of Anionic Surfactants on the Water Permeability of a Model Stratum Corneum Lipid Membrane
journal, December 2013
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- Langmuir, Vol. 30, Issue 1
Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
journal, December 2000
- Morgan, Dave; Diamond, David M.; Gottschall, Paul E.
- Nature, Vol. 408, Issue 6815
Amyloid-β forms fibrils by nucleated conformational conversion of oligomers
journal, July 2011
- Lee, Jiyong; Culyba, Elizabeth K.; Powers, Evan T.
- Nature Chemical Biology, Vol. 7, Issue 9
The amyloid state and its association with protein misfolding diseases
journal, May 2014
- Knowles, Tuomas P. J.; Vendruscolo, Michele; Dobson, Christopher M.
- Nature Reviews Molecular Cell Biology, Vol. 15, Issue 6
Diffusion in single supported lipid bilayers studied by quasi-elastic neutron scattering
journal, January 2010
- Armstrong, Clare L.; Kaye, Martin D.; Zamponi, Michaela
- Soft Matter, Vol. 6, Issue 23
The dynamical landscape in CTAB micelles
journal, January 2012
- Sharma, V. K.; Mitra, S.; Garcia Sakai, V.
- Soft Matter, Vol. 8, Issue 27
Differences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease
journal, January 2014
- Kotler, Samuel A.; Walsh, Patrick; Brender, Jeffrey R.
- Chem. Soc. Rev., Vol. 43, Issue 19
A neutron scattering study of the structure of a bimodal colloidal crystal
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