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Multistep tandem mass spectrometry for Sequencing Cyclic Peptides in an Ion-Trap Mass Spectrometer

  • Lambert C. M. Ngoka
  • Michael L. GrossEmail author
Articles

Abstract

Collisionally activated decomposition (CAD) of a protonated cyclic peptide produces a superposition spectrum consisting of fragments produced following random ring opening of the cyclic peptide to give a set of acylium ions (or isomeric equivalents) of the same m/z. Assignment of the correct sequence is often difficult owing to lack of selectivity in the ring opening. A method is presented that utilizes multiple stages of CAD experiments in an electrospray ion-trap mass spectrometer to sequence cyclic peptides. A primary acylium ion is selected from the primary product-ion spectrum and subjected to several stages of CAD. Amino-acid residues are sequentially removed, one at each stage of the CAD, from the C-terminus, until a b2 ion is reached. Results are presented for seven cyclic peptides, ranging in sizes from four to eight amino-acid residues. This method of sequencing cyclic peptides eliminates ambiguities encountered with other MS/MS approaches. The power of the strategy lies in the capability to execute several stages of CAD upon a precursor ion and its decomposition products, allowing the cyclic peptide to be sequenced in an unambiguous, stepwise manner.

Keywords

Cyclic Peptide Collisional Activation Tentoxin Collisionally Activate Decomposition Spectrum Isomeric Equivalent 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© American Society for Mass Spectrometry 1999

Authors and Affiliations

  1. 1.Department of ChemistryWashington University in St. LouisSt. Louis

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