Evidence map›Paper›PMID 19873993›Full record

ArticleAnalytical chemistry2009

Identification of aspartic and isoaspartic acid residues in amyloid beta peptides, including Abeta1-42, using electron-ion reactions.

Nadezda P Sargaeva, Cheng Lin, Peter B O'Connor

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

34 citing papers in PubMed, 83 citations in OpenAlex.

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  17. In-Source Decay Characterization of Isoaspartate and β-Peptides.International journal of mass spectrometry · 2015
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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

3 authors at 1 institution in 1 country.

Nadezda P SargaevaMass Spectrometry Resource, Department of Biochemistry, Boston University School of Medicine, 670 Albany Street, R504, Boston, Massachusetts 02118, USA.
Cheng Lin
Peter B O'Connor
University of Warwick · GB

Funding

XI INTERNATIONAL SYMPOSIUM ON AMYLOIDOSISP41RR010888 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 1996 to 2011
$18.6M
Defining the IsoAspartomeR01GM078293 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LIN, CHENG · 2007 to 2011
$1.5M
NHLBI PROTEOMICS INITIATIVE-N01HV28178N01HV028178 · HV · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2002 to 2006
–
STRUCTURAL CHARACTERIZATION OF THE APOPROTEIN E RECEPTORR01HL028178 · NHLBI · J. DAVID GLADSTONE INSTITUTES · PI INNERARITY, THOMAS L. · 1986 to 1988
–
NCRR NIH HHS P41 RR010888NCRR NIH HHS P41 RR10888NHLBI NIH HHS N01 HV028178NIGMS NIH HHS R01 GM078293NIGMS NIH HHS R01GM078293
6 · The paper itself

Abstract

Amyloid beta peptides are the major components of the vascular and plaque amyloid filaments in individuals with Alzheimer's disease (AD). Although it is still unclear what initiates the disease, isomerization of aspartic acid residues in Abeta peptides is directly related to the pathology of AD. The detection of isomerization products is analytically challenging, due to their similar chemical properties and identical molecular mass. Different methods have been applied to differentiate and quantify the isomers, including immunology, chromatography, and mass spectrometry. Typically, those methods require comparative analysis with the standard peptides and involve many sample preparation steps. To understand the role of Abeta isomerization in AD progression, a fast, simple, accurate, and reproducible method is necessary. In this work, electron capture dissociation (ECD) Fourier-transform ion cyclotron resonance mass spectrometry (FTICR MS) was applied to detect isomerization in Abeta peptides. ECD generated diagnostic fragment ions for the two isomers of Abeta17-28, [M + 2H - 60]+* and z6*-44 when aspartic acid was present and z6*-57 when isoaspartic acid was present. Additionally, the z(n)-57 diagnostic ion was also observed in the electron ionization dissociation (EID) spectra of the modified Abeta17-28 fragment. ECD was further applied toward Abeta1-40 and Abeta1-42. The diagnostic ion c6 + 57 was observed in the ECD spectra of the Abeta1-42 peptide, demonstrating isomerization at residue 7. In conclusion, both ECD and EID can clearly determine the presence and the position of isoaspartic acid residues in amyloid beta peptides. The next step, therefore, is to apply this method to analyze samples of Alzheimer's patients and healthy individuals in order to generate a better understanding of the disease.

Indexed as

ElectronsAmino Acid SequenceAmyloid beta-PeptidesAnalytic Sample Preparation MethodsAspartic AcidFourier AnalysisHydrophobic and Hydrophilic InteractionsIsoaspartic AcidIsomerismMass SpectrometryPeptide FragmentsTime FactorsAmyloid beta-Peptidesamyloid beta-protein (1-42)Aspartic AcidIsoaspartic AcidPeptide Fragments

Identifiers

PMID19873993
PMCPMC3114306
OpenAlexW2165096868

What OpenQuestion holds

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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.