These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Formation of diagnostic product ions from cyanobacterial cyclic peptides by the two-bond fission mechanism using ion trap liquid chromatography/multi-stage mass spectrometry.
    Author: Mayumi T, Kato H, Kawasaki Y, Harada K.
    Journal: Rapid Commun Mass Spectrom; 2007; 21(6):1025-33. PubMed ID: 17318805.
    Abstract:
    Product ions obtained by tandem mass spectrometry (MS/MS) are quite effective for the amino acid sequencing of linear peptides. However, in the case of cyclic peptides, the fragmentation pattern is complicated because the cleavages occur randomly and product ions are generated as a(n), b(n), c(n), x(n), y(n) and z(n) series ions; therefore, the authors have never obtained sufficient sequence information. In order to overcome this problem, we applied ion trap liquid chromatography/multi-stage mass spectrometry (LC/MS(n)) and characterized the product ions obtained from anabaenopeptins and aeruginopeptins as the cyclic peptides. For the anabaenopeptins, MS(2) analysis did not provide sufficient sequence information on the cyclic structure, and MS(3) analysis was applied to sequence the constituent amino acids. Diagnostic product ions were obtained by the MS(3) analysis and were quite effective for obtaining the sequence information of the constituent amino acids. MS(2) analysis was, however, sufficient to obtain the sequence information of the aeruginopeptins. In both cases, the resulting product ions obtained from the cyclic structures were formed by the two-bond fission mechanism of the precursor ion, in which an initial fission of the cyclic structure to a linear one and subsequent fission(s) at the peptide bonds are included. The fragmentations were similar for the structurally related compounds, indicating that the cleavages occurred at definite peptide bonds. In addition, the resulting product ions are generated as b(n) series ions and the mass difference facilitates the amino acid sequencing. Thus, ion trap LC/MS(n) provides sequence information, and the resulting product ions are reproducible among the structurally related compounds and reliable for the sequencing of the constituent amino acids of the cyclic structure.
    [Abstract] [Full Text] [Related] [New Search]