Extraribosomal cyclic tetradepsipeptides beauverolides: profiling and modeling the fragmentation pathways
Language English Country Great Britain, England Media print
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
PubMed
15329847
DOI
10.1002/jms.674
Knihovny.cz E-resources
- MeSH
- Biomarkers analysis MeSH
- Peptides, Cyclic analysis chemistry metabolism MeSH
- Depsipeptides * MeSH
- Species Specificity MeSH
- Spectrometry, Mass, Electrospray Ionization MeSH
- Fungi classification metabolism MeSH
- Peptides chemistry MeSH
- Protons MeSH
- Ribosomes metabolism MeSH
- Chromatography, High Pressure Liquid MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- beauverolides MeSH Browser
- Biomarkers MeSH
- Peptides, Cyclic MeSH
- Depsipeptides * MeSH
- Peptides MeSH
- Protons MeSH
Profiling of cyclic tetradepsipeptides beauverolides was tested as a chemotaxonomic tool for fungal strain identification/discrimination. Two new tetradepsipeptides, beauverolides Q and R, were characterized by tandem mass spectrometry. Specific elimination of 113 atomic mass units from both protonated and sodiated molecules of beauverolides is ubiquitous for all 12 most dominant congeners evaluated in this profiling study. Reconstruction of the total ion chromatogram, according to this neutral fragment release, was used for data filtering and selectivity enhancement. Selective ring opening and fragment ion formation of beauverolide I are discussed in detail utilizing high-level theoretical modeling of the fragmentation pathways.
References provided by Crossref.org
CYCLONE--a utility for de novo sequencing of microbial cyclic peptides
