Self-assembly of the full-length amyloid Aβ42 protein in dimers

Zhang, Yuliang; Hashemi, Mohtadin; Lv, Zhengjian; Lyubchenko, Yuri L.

doi:10.1039/c6nr06850b

Self-assembly of the full-length amyloid Aβ42 protein in dimers

Journal Article · Thu Sep 29 00:00:00 EDT 2016 · Nanoscale

DOI:https://doi.org/10.1039/c6nr06850b· OSTI ID:1879279

Zhang, Yuliang ^[1]; Hashemi, Mohtadin ^[2]; Lv, Zhengjian ^[2]; Lyubchenko, Yuri L. ^[2]

University of Nebraska Medical Center, Omaha, NE (United States); Lawrence Livermore National Lab. (LLNL), Livermore, CA (United States)
University of Nebraska Medical Center, Omaha, NE (United States)

The self-assembly of amyloid (Aβ) proteins into nano-aggregates is a hallmark of Alzheimer’s disease (AD) development, yet the mechanism of how disordered monomers assemble into aggregates remains elusive. Here, we applied long-time molecular dynamics simulations to fully characterize the assembly of Aβ42 monomers into dimers. Monomers undergo conformational changes during their interaction, but the resulting dimer structures do not resemble those found in fibril structures. Further, to identify natural conformations of dimers among a set of simulated ones, validation approaches were developed and applied, and a subset of dimer conformations were characterized. These dimers do not contain long β-strands that are usually found in fibrils. The dimers are stabilized primarily by interactions within the central hydrophobic regions and the C-terminal regions, with a contribution from local hydrogen bonding. The dimers are dynamic, as evidenced by the existence of a set of conformations and by the quantitative analyses of the dimer dissociation process.

View Accepted Manuscript (DOE)

Research Organization:: Lawrence Livermore National Laboratory (LLNL), Livermore, CA (United States)

Sponsoring Organization:: National Institutes of Health (NIH); National Science Foundation (NSF); USDOE National Nuclear Security Administration (NNSA)

Grant/Contract Number:: AC52-07NA27344

OSTI ID:: 1879279

Report Number(s):: LLNL-JRNL-837698; 1057615

Journal Information:: Nanoscale, Journal Name: Nanoscale Journal Issue: 45 Vol. 8; ISSN 2040-3364

Publisher:: Royal Society of ChemistryCopyright Statement

Country of Publication:: United States

Language:: English

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