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 int
Sequencing of a branched peptide using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
✍ Scribed by I. Fournier; P. Chaurand; G. Bolbach; F. Lützenkirchen; B. Spengler; J. C. Tabet
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 163 KB
- Volume
- 35
- Category
- Article
- ISSN
- 1076-5174
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✦ Synopsis
Chemical degradation methods combined with matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and post-source decay (PSD)-MALDI reflex TOF mass spectrometry (MS) were used to determine the sequence of a peptide branched on to a known peptide backbone. This study was applied to a branched peptide model (derivative of substance P). The branched peptide mimics a digest of a membrane receptor on to which a derivative of substance P was photochemically linked. Chemical degradation based on N-terminal ladder sequencing in combination with MALDI-TOF-MS gave only partial sequence information. Although single PSD mass spectra still remain difficult to interpret unambiguously, PSD-MALDI-TOF-MS was combined with on-target acetylation and H -- D exchange to give a better and successful approach to the unambiguous determination of the complete amino acid side-chain sequence. This study shows the capability of MALDI-TOF-MS to help in characterizing ligand-receptor interactions.
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