Evidence map›Paper›PMID 25928376›Full record

ArticlePloS one2015

Nanoscale Synaptic Membrane Mimetic Allows Unbiased High Throughput Screen That Targets Binding Sites for Alzheimer's-Associated Aβ Oligomers.

Kyle C Wilcox, Matthew R Marunde, Aditi Das, Pauline T Velasco, Benjamin D Kuhns, Michael T Marty, Haoming Jiang, Chi-Hao Luan, Stephen G Sligar, William L Klein

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.4field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Review
  3. Nanodiscs: A toolkit for membrane protein science.Protein science : a publication of the Protein Society · 2021
    Review
  4. Nanodiscs and Mass Spectrometry: Making Membranes Fly.International journal of mass spectrometry · 2020
    Article
  5. Article
  6. Profiling theeLife · 2019
    Article
  7. The hydrodynamic motion of Nanodiscs.Chemistry and physics of lipids · 2019
    Article
  8. Review
  9. Review
  10. Cellular Receptors of Amyloid β Oligomers (AβOs) in Alzheimer's Disease.International journal of molecular sciences · 2018
    Review
  11. Article
  12. The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade.Journal of Alzheimer's disease : JAD · 2018
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Kyle C WilcoxDepartment of Neurobiology, Northwestern University, Evanston, IL, United States of America.
Matthew R MarundeDepartment of Neurobiology, Northwestern University, Evanston, IL, United States of America.
Aditi DasDepartment of Comparative Biosciences, University of Illinois-Urbana Champaign, Urbana, IL, United States of America; Department of Biochemistry, University of Illinois-Urbana Champaign, Urbana, IL, United States of America.
Pauline T VelascoDepartment of Neurobiology, Northwestern University, Evanston, IL, United States of America.
Benjamin D KuhnsDepartment of Neurobiology, Northwestern University, Evanston, IL, United States of America.
Michael T MartyDepartment of Chemistry, University of Illinois-Urbana Champaign, Urbana, IL, United States of America.
Haoming JiangDepartment of Neurobiology, Northwestern University, Evanston, IL, United States of America.
Chi-Hao LuanHigh Throughput Analysis Laboratory and Department of Molecular Biosciences, Northwestern University, Evanston, IL, United States of America.
Stephen G SligarDepartment of Biochemistry, University of Illinois-Urbana Champaign, Urbana, IL, United States of America; Department of Chemistry, University of Illinois-Urbana Champaign, Urbana, IL, United States of America.
William L KleinDepartment of Neurobiology, Northwestern University, Evanston, IL, United States of America.
Northwestern University · USUniversity of Illinois Urbana-Champaign · USHigh Throughput Biology (United States) · US

Funding

PREDOCTORAL AND POSTDOCTORAL TRAINING PROGRAM IN AGING AND DEMENTIAT32AG020506 · NIA · NORTHWESTERN UNIVERSITY AT CHICAGO · PI ROBERT J VASSAR, SANDRA WEINTRAUB · 2002 to 2026
$9.9M
Nanoscale Approaches to Understanding Membrane Protein FunctionR35GM118145 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI STEPHEN G. SLIGAR · 2016 to 2026
$7.5M
METALLOENZYME MECHANISMSR01GM033775 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 1985 to 2014
$5.2M
Abeta oligomers (ADDLs)in Alzheimers Disease pathologyR01AG022547 · NIA · NORTHWESTERN UNIVERSITY · PI KLEIN, WILLIAM L · 2003 to 2010
$1.9M
ADDLs, synapses & the molecular etiology of Alzheimer's diseaseR01AG029460 · NIA · NORTHWESTERN UNIVERSITY · PI KLEIN, WILLIAM L · 2007 to 2009
$916k
Alzheimer's Drug Discovery Using Unique Nanotechnology PlatformR21AG041953 · NIA · NORTHWESTERN UNIVERSITY · PI KLEIN, WILLIAM L · 2012 to 2013
$432k
Soluble Membrane Protein Libraries: Design and use in Alzheimers drug discoveryF32AG039171 · NIA · NORTHWESTERN UNIVERSITY · PI WILCOX, KYLE CHRISTOPHER · 2011 to 2012
$105k
NIA NIH HHS AG020506NIA NIH HHS AG022547NIA NIH HHS AG029460NIA NIH HHS AG039171NIA NIH HHS AG041953NIA NIH HHS F32 AG039171NIA NIH HHS R01 AG022547NIA NIH HHS R01 AG029460NIA NIH HHS R21 AG041953NIA NIH HHS T32 AG020506NIGMS NIH HHS GM33775NIGMS NIH HHS R01 GM033775NIGMS NIH HHS R35 GM118145
6 · The paper itself

Abstract

Despite their value as sources of therapeutic drug targets, membrane proteomes are largely inaccessible to high-throughput screening (HTS) tools designed for soluble proteins. An important example comprises the membrane proteins that bind amyloid β oligomers (AβOs). AβOs are neurotoxic ligands thought to instigate the synapse damage that leads to Alzheimer's dementia. At present, the identities of initial AβO binding sites are highly uncertain, largely because of extensive protein-protein interactions that occur following attachment of AβOs to surface membranes. Here, we show that AβO binding sites can be obtained in a state suitable for unbiased HTS by encapsulating the solubilized synaptic membrane proteome into nanoscale lipid bilayers (Nanodiscs). This method gives a soluble membrane protein library (SMPL)--a collection of individualized synaptic proteins in a soluble state. Proteins within SMPL Nanodiscs showed enzymatic and ligand binding activity consistent with conformational integrity. AβOs were found to bind SMPL Nanodiscs with high affinity and specificity, with binding dependent on intact synaptic membrane proteins, and selective for the higher molecular weight oligomers known to accumulate at synapses. Combining SMPL Nanodiscs with a mix-incubate-read chemiluminescence assay provided a solution-based HTS platform to discover antagonists of AβO binding. Screening a library of 2700 drug-like compounds and natural products yielded one compound that potently reduced AβO binding to SMPL Nanodiscs, synaptosomes, and synapses in nerve cell cultures. Although not a therapeutic candidate, this small molecule inhibitor of synaptic AβO binding will provide a useful experimental antagonist for future mechanistic studies of AβOs in Alzheimer's model systems. Overall, results provide proof of concept for using SMPLs in high throughput screening for AβO binding antagonists, and illustrate in general how a SMPL Nanodisc system can facilitate drug discovery for membrane protein targets.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsBinding SitesIn Vitro TechniquesProtein BindingRatsSynaptic MembranesSynaptosomesAmyloid beta-Peptides

Identifiers

PMID25928376
PMCPMC4415972
OpenAlexW1976154364

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.