Infrared Multiphoton Dissociation for Enhanced de Novo Sequence Interpretation of N-Terminal Sulfonated Peptides in a Quadrupole Ion Trap
peer-reviewed · Analytical Chemistry · 2006
| Date | 2006-10-01 |
| Type | peer-reviewed |
| Venue | Analytical Chemistry |
| Publisher | American Chemical Society (ACS) |
| Contribution | algorithm |
| DOI | 10.1021/ac060760d |
| Citations (OpenAlex) | 41 |
| Venue 2-year citedness | 7.10 |
Abstract
Infrared multiphoton dissociation (IRMPD) of N-terminal sulfonated peptides improves de novo sequencing capabilities in a quadrupole ion trap mass spectrometer. Not only does IRMPD promote highly efficient dissociation of the N-terminal sulfonated peptides but also the entire series of y ions down to the y(1) fragment may be detected due to alleviation of the low-mass cutoff problem associated with conventional collisional activated dissociation (CAD) methods in a quadrupole ion trap. Commercial de novo sequencing software was applied for the interpretation of CAD and IRMPD MS/MS spectra collected for seven unmodified peptides and the corresponding N-terminal sulfonated species. In most cases, the additional information obtained by N-terminal sulfonation in combination with IRMPD provided significant improvements in sequence identification. The software sequence tag results were combined with a commercial database searching algorithm to interpret sequence information of a tryptic digest on alpha-casein s1. Energy-variable CAD studies confirmed a 30-40% reduction in the critical energies of the N-terminal sulfonated peptides relative to unmodified peptides. This reduction in dissociation energy facilitates IRMPD in a quadrupole ion trap.
Methods and tools
- IRMPD of N-terminal sulfonated peptides: Infrared multiphoton dissociation of N-terminal sulfonated peptides in a quadrupole ion trap, which both dissociates them efficiently and carries the y-ion series all the way down to y1, so the C-terminal residue is not lost.
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