MALDI TOF/TOF-based approach for the identification of d-amino acids in biologically active peptides and proteins

Koehbach, Johannes, Gruber, Christian W., Becker, Christian, Kreil, David P. and Jilek, Alexander (2016) MALDI TOF/TOF-based approach for the identification of d-amino acids in biologically active peptides and proteins. Journal of Proteome Research, 15 5: 1487-1496. doi:10.1021/acs.jproteome.5b01067


Author Koehbach, Johannes
Gruber, Christian W.
Becker, Christian
Kreil, David P.
Jilek, Alexander
Title MALDI TOF/TOF-based approach for the identification of d-amino acids in biologically active peptides and proteins
Journal name Journal of Proteome Research   Check publisher's open access policy
ISSN 1535-3907
1535-3893
Publication date 2016-05-06
Year available 2016
Sub-type Article (original research)
DOI 10.1021/acs.jproteome.5b01067
Open Access Status DOI
Volume 15
Issue 5
Start page 1487
End page 1496
Total pages 10
Place of publication Washington, DC, United States
Publisher American Chemical Society
Collection year 2017
Language eng
Formatted 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.
Keyword Chirality
D - amino acid containing peptide
Isotope label
Peptidomics
Post-translational modification
Proteomics
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
School of Biomedical Sciences Publications
 
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