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Mass spectrometric fragmentation of cyclic peptides belonging to the polymyxin and colistin antibiotics studied by ion trap and quadrupole/orthogonal‐acceleration time‐of‐flight technology
Author(s) -
Govaerts Cindy,
Rozenski Jef,
Orwa Jennifer,
Roets Eugène,
Schepdael Ann Van,
Hoogmartens Jos
Publication year - 2002
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.644
Subject(s) - chemistry , fragmentation (computing) , quadrupole , polymyxin , chromatography , quadrupole time of flight , ion , ion trap , quadrupole ion trap , polymyxin b , analytical chemistry (journal) , antibiotics , acceleration , mass spectrometry , organic chemistry , atomic physics , tandem mass spectrometry , biochemistry , physics , classical mechanics , computer science , operating system
Electrospray ionization linked to quadrupole/orthogonal‐acceleration time‐of‐flight (Q/oaTOF) and ion trap equipment was used to study the fragmentation behavior of the linear side‐chain cyclized peptides of the polymyxin B and E antibiotics. This study exemplifies both the benefits and the drawbacks of mass spectrometric techniques for the determination of the sequence of such complex linear side‐chain cyclized peptides. Q/oaTOF accurate mass measurements did not help sufficiently to assign the product ions observed in the product ion spectra. An ion trap mass spectrometer providing MS n capability was used to eliminate ambiguities encountered with a single MS/MS approach. The complex fragmentation behavior of these compounds of well‐established structure is described which could be useful for structural characterization of unknown substances related to polymyxin B and E in the future. Copyright © 2002 John Wiley & Sons, Ltd.