A series of synthetic cyclic decapeptides and other smaller cyclic peptides were analyzed using matrixassisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry. The investigated compounds were cyclized in a head-to-tail manner and contained non-proteinaceous amino acids, such
Accurate peptide sequencing by post-source decay matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
β Scribed by Wenjun Mo; Toshifumi Takao; Yasutsugu Shimonishi
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 153 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0951-4198
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β¦ Synopsis
Partial 18 O-labeling of peptides has been applied to post-source decay experiments in a matrix-assisted laser desorption/ionization time-of-flight mass spectrometer. The ions which originate from the carboxyl terminus of a peptide partially retain 18 O atoms which have readily been incorporated into the C-terminal carboxyl groups during enzymatic hydrolysis in a buffer containing 40 atom percent H 2 18 O. The isotopic resolution of singly charged precursor ions and their product ions obtained for peptides up to ca. 2800 Da has been achieved using the delayed extraction method, which permits the rapid identification and assignment of the 18 O-labeled and non-labeled ion species in the PSD spectra. The results obtained from several 18 O-labeled peptides, derived from an enzymatic digest, demonstrate the accuracy and reproducibility of the present method, which will be in widespread use for protein identification via database searching or for investigations of totally unknown proteins.
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