Evidence map›Paper›PMID 23612608›Full record

ArticlePhysical chemistry chemical physics : PCCP2013

Amyloid-β-neuropeptide interactions assessed by ion mobility-mass spectrometry.

Molly T Soper, Alaina S DeToma, Suk-Joon Hyung, Mi Hee Lim, Brandon T Ruotolo

Abstract read
In one paragraph

Article in Physical chemistry chemical physics : PCCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  6. SERF engages in a fuzzy complex that accelerates primary nucleation of amyloid proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
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  18. Advances in Mass Spectrometric Tools for Probing Neuropeptides.Annual review of analytical chemistry (Palo Alto, Calif.) · 2015
    Review
  19. 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

5 authors at 1 institution in 1 country.

Molly T SoperDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
Alaina S DeToma
Suk-Joon Hyung
Mi Hee Lim
Brandon T Ruotolo
University of Michigan–Ann Arbor · US

Funding

Next-generation Mass Spectrometry Technologies for Integrated Structural Proteomics- RenewalR01GM095832 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RUOTOLO, BRANDON T · 2011 to 2024
$5.8M
Proteogenomics of Cancer Training ProgramT32CA140044 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAO, ARVIND, SARTOR, MAUREEN AGNES · 2010 to 2024
$3.9M
NCI NIH HHS T32 CA140044NIGMS NIH HHS GM-095832NIGMS NIH HHS R01 GM095832
6 · The paper itself

Abstract

Recently, small peptides have been shown to modulate aggregation and toxicity of the amyloid-β protein (Aβ). As such, these new scaffolds may help discover a new class of biotherapeutics useful in the treatment of Alzheimer's disease. Many of these inhibitory peptide sequences have been derived from natural sources or from Aβ itself (e.g., C-terminal Aβ fragments). In addition, much earlier work indicates that tachykinins, a broad class of neuropeptides, display neurotrophic properties, presumably through direct interactions with either Aβ or its receptors. Based on this work, we undertook a limited screen of neuropeptides using ion mobility-mass spectrometry to search for similar such peptides with direct Aβ binding properties. Our results reveal that the neuropeptides leucine enkephalin (LE) and galanin interact with both the monomeric and small oligomeric forms of Aβ(1-40) to create a range of complexes having diverse stoichiometries, while some tachyknins (i.e., substance P) do not. LE interacts with Aβ more strongly than galanin, and we utilized ion mobility-mass spectrometry, molecular dynamics simulations, gel electrophoresis/Western blot, and transmission electron microscopy to study the influence of this peptide on the structure of Aβ monomer, small Aβ oligomers, as well as the eventual formation of Aβ fibrils. We find that LE binds selectively within a region of Aβ between its N-terminal tail and hydrophobic core. Furthermore, our data indicate that LE modulates fibril generation, producing shorter fibrillar aggregates when added in stoichiometric excess relative to Aβ.

Indexed as

Alzheimer DiseaseAmino Acid SequenceAmyloid beta-PeptidesBinding SitesEnkephalin, LeucineGalaninHumansHydrophobic and Hydrophilic InteractionsMass SpectrometryMolecular Docking SimulationMolecular Dynamics SimulationMolecular Sequence DataProtein BindingTachykininsAmyloid beta-PeptidesEnkephalin, LeucineGalaninTachykinins

Identifiers

PMID23612608
PMCPMC3664942
OpenAlexW2069071040

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.