Multistep tandem mass spectrometry for sequencing cyclic peptides in an ion-trap mass spectrometer
| Autor: | Michael L. Gross, Lambert C. M. Ngoka |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Endothelin Receptor Antagonists
Electrospray Analytical chemistry Protonation Spectrometry Mass Fast Atom Bombardment 010402 general chemistry Tandem mass spectrometry Ring (chemistry) Mass spectrometry 01 natural sciences Peptides Cyclic Mass Spectrometry Ion Surface-Active Agents Structural Biology Amino Acid Sequence Amino Acids Spectroscopy chemistry.chemical_classification 010401 analytical chemistry Receptor Endothelin A Combinatorial chemistry Cyclic peptide 0104 chemical sciences chemistry Ion trap |
| Zdroj: | Journal of the American Society for Mass Spectrometry. 10(8) |
| ISSN: | 1044-0305 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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