Spontaneous self-assembly of amyloid β (1–40) into dimers

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

doi:10.1039/c9na00380k

Title: Spontaneous self-assembly of amyloid β (1–40) into dimers

Journal Article · 17 September 2019 · Nanoscale Advances

DOI: https://doi.org/10.1039/c9na00380k · OSTI ID:1661023

^[1]; Zhang, Yuliang ^[2]; Lv, Zhengjian ^[3];

^[1]

Univ. of Nebraska Medical Center, Omaha, NE (United States)
Univ. of Nebraska Medical Center, Omaha, NE (United States); Lawrence Livermore National Lab. (LLNL), Livermore, CA (United States)
Univ. of Nebraska Medical Center, Omaha, NE (United States); Bruker Nano Surfaces Division, Santa Barbara, CA (United States)

The self-assembly and fibrillation of amyloid β (Aβ) proteins is the neuropathological hallmark of Alzheimer's disease. However, the molecular mechanism of how disordered monomers assemble into aggregates remains largely unknown. In this work, we characterize the assembly of Aβ (1–40) monomers into dimers using long-time molecular dynamics simulations. Upon interaction, the monomers undergo conformational transitions, accompanied by change of the structure, leading to the formation of a stable dimer. The dimers are stabilized by interactions in the N-terminal region (residues 5–12), in the central hydrophobic region (residues 16–23), and in the C-terminal region (residues 30–40); with inter-peptide interactions focused around the N- and C-termini. The dimers do not contain long β-strands that are usually found in fibrils.

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

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

Grant/Contract Number:: AC52-07NA27344; GM096039; GM100156; 1004094; ACI-1053575; R01GM116961

OSTI ID:: 1661023

Report Number(s):: LLNL-JRNL-813715; 1021710

Journal Information:: Nanoscale Advances, Vol. 1, Issue 10; ISSN 2516-0230

Publisher:: Royal Society of ChemistryCopyright Statement

Country of Publication:: United States

Language:: English

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