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 | Zendy

Govaerts Cindy | Zendy; Rozenski Jef | Zendy; Orwa Jennifer | Zendy; Roets Eugène | Zendy; Schepdael Ann Van | Zendy; Hoogmartens Jos | Zendy

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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.

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