Evidence map›Paper›PMID 26985971›Full record

ArticleJournal of proteome research2016

MALDI TOF/TOF-Based Approach for the Identification of d- Amino Acids in Biologically Active Peptides and Proteins.

Johannes Koehbach, Christian W Gruber, Christian Becker, David P Kreil, Alexander Jilek

Abstract read
In one paragraph

Article in Journal of proteome research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Review
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  13. Advancing d-amino acid-containing peptide discovery in the metazoan.Biochimica et biophysica acta. Proteins and proteomics · 2021
    Review
  14. Methods of Measuring Enzyme Activity Ex Vivo and In Vivo.Annual review of analytical chemistry (Palo Alto, Calif.) · 2018
    Review
  15. Article
  16. Article
  17. Review
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.

Johannes KoehbachCentre for Physiology and Pharmacology, Medical University of Vienna , Schwarzspanierstraße 17, A-1090 Vienna, Austria.
Christian W GruberCentre for Physiology and Pharmacology, Medical University of Vienna , Schwarzspanierstraße 17, A-1090 Vienna, Austria.
Christian BeckerInstitute of Biological Chemistry, Department of Chemistry, University of Vienna , Währinger Straße 38, A-1090 Vienna, Austria.
David P KreilChair of Bioinformatics, University of Natural Resources and Life Sciences , Muthgasse 18, A-1190 Vienna, Austria.
Alexander JilekInstitute of Biological Chemistry, Department of Chemistry, University of Vienna , Währinger Straße 38, A-1090 Vienna, Austria.

Funding

Austrian Science Fund FWF P 22889Austrian Science Fund FWF P 24743
6 · The paper itself

Abstract

Several biologically active peptides contain a d- amino acid in a well-defined position, which is position 2 in all peptide epimers isolated to date from vertebrates and also some from invertebrates. The detection of such D- residues by standard analytical techniques is challenging. In tandem mass spectrometric (MS) analysis, although fragment masses are the same for all stereoisomers, peak intensities are known to depend on chirality. Here, we observe that the effect of a d- amino acid in the second N-terminal position on the fragmentation pattern in matrix assisted laser desorption time-of-flight spectrometry (MALDI-TOF/TOF MS) strongly depends on the peptide sequence. Stereosensitive fragmentation (SF) is correlated to a neighborhood effect, but the d- residue also exerts an overall effect influencing distant bonds. In a fingerprint analysis, multiple peaks can thus serve to identify the chirality of a sample in short time and potentially high throughput. Problematic variations between individual spots could be successfully suppressed by cospotting deuterated analogues of the epimers. By identifying the [d-Leu2] isomer of the predicted peptide GH-2 (gene derived bombininH) in skin secretions of the toad Bombina orientalis, we demonstrated the analytical power of SF-MALDI-TOF/TOF measurements. In conclusion, SF-MALDI-TOF/TOF MS combines high sensitivity, versatility, and the ability to complement other methods.

Indexed as

StereoisomerismAmino AcidsAnimalsAntimicrobial Cationic PeptidesAnuraDeuteriumPeptidesProteinsSkinSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationAmino AcidsAntimicrobial Cationic Peptidesbombinin H2DeuteriumPeptidesProteinschiralityd- amino acid containing peptideisotope labelpeptidomicspost-translational modificationproteomics

Identifiers

PMID26985971
PMCPMC4861975

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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.