Neutron Scattering Studies of the Interplay of Amyloid β Peptide(1–40) and An Anionic Lipid 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-11

AUTHORS

Durgesh K Rai, Veerendra K Sharma, Divina Anunciado, Hugh O'Neill, Eugene Mamontov, Volker Urban, William T Heller, Shuo Qian

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. More... »

PAGES

30983

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep30983

DOI

http://dx.doi.org/10.1038/srep30983

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1008573354

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27503057


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