Inhibition of Amyloid β-Induced Lipid Membrane Permeation and&nbsp;Amyloid β Aggregation by K162

Mrdenovic, Dusan; Zarzycki, Piotr; Majewska, Marta; Pieta, Izabela S.; Nowakowski, Robert; Kutner, Wlodzimierz; Lipkowski, Jacek; Pieta, Piotr

doi:10.1021/acschemneuro.0c00754

Inhibition of Amyloid β-Induced Lipid Membrane Permeation and Amyloid β Aggregation by K162

Journal Article · Thu Jan 21 23:00:00 EST 2021 · ACS Chemical Neuroscience

DOI:https://doi.org/10.1021/acschemneuro.0c00754· OSTI ID:1810820

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Polish Academy of Sciences (PAS), Warsaw (Poland); Univ. of Guelph, ON (Canada)
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Polish Academy of Sciences (PAS), Warsaw (Poland)
Polish Academy of Sciences (PAS), Warsaw (Poland); Cardinal Stefan Wyszynski Univ., Warsaw (Poland)
Univ. of Guelph, ON (Canada)

Alzheimer's disease (AD) is characterized by progressive neurodegeneration associated with amyloid β (Aβ) peptide aggregation. The aggregation of Aβ monomers (AβMs) leads to the formation of Aβ oligomers (AβOs), the neurotoxic Aβ form, capable of permeating the cell membrane. Here, we investigated the effect of a fluorene-based active drug candidate, named K162, on both Aβ aggregation and AβO toxicity toward the bilayer lipid membrane (BLM). Electrochemical impedance spectroscopy (EIS), atomic force microscopy (AFM), and molecular dynamics (MD) were employed to show that K162 inhibits AβOs-induced BLM permeation, thus preserving BLM integrity. In the presence of K162, only shallow defects on the BLM surface were formed. Apparently, K162 modifies Aβ aggregation by bypassing the formation of toxic AβOs, and only nontoxic AβMs, dimers (AβDs), and fibrils (AβFs) are produced. Unlike other Aβ toxicity inhibitors, K162 preserves neurologically beneficial AβMs. This unique K162 inhibition mechanism provides an alternative AD therapeutic strategy that could be explored in the future.

View Accepted Manuscript (DOE)

Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division; Polish National Science Centre (NCN); Polish Academy of Sciences; Natural Sciences and Engineering Research Council of Canada (NSERC); European Research Council (ERC)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1810820

Journal Information:: ACS Chemical Neuroscience, Journal Name: ACS Chemical Neuroscience Journal Issue: 3 Vol. 12; ISSN 1948-7193

Publisher:: American Chemical Society (ACS)Copyright Statement

Country of Publication:: United States

Language:: English

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Alzheimer’s disease
amyloid β
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atomic force microscopy
membrane permeation
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Inhibition of Amyloid β-Induced Lipid Membrane Permeation and Amyloid β Aggregation by K162

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