Infrared Multiphoton Dissociation Spectroscopic Analysis of Peptides and Oligosaccharides by Using Fourier Transform Ion Cyclotron Resonance Mass Spectrometry with a Midinfrared Free-Electron Laser

Abstract

The fragmentation of peptides and oligosaccharides in the gas phase was investigated by means of electrospray ionization Fourier transform ion cyclotron resonance (FTICR) mass spectrometry coupled with dissociation by a laser-cleavage infrared multiphoton dissociation (IRMPD) technique. In this technique, an IR free-electron laser is used as a tunable source of IR radiation to cause cleavage of the ionized samples introduced into the FTICR cell. The gas-phase IRMPD spectra of protonated peptides (substance P and angiotensin II) and two sodiated oligosaccharides (sialyl Lewis X and lacto-N-fucopentaose III) were obtained over the IR scan range of 5.7-9.5 microm. In the IRMPD spectra for the peptide, fragment ions are observed as y/b-type fragment ions in the range 5.7-7.5 microm, corresponding to cleavage of the backbone of the parent amino acid sequence, whereas the spectra of the oligosaccharides have major peaks in the range 8.4-9.5 microm, corresponding to photoproducts of the B/Y type.

Assembly and remodeling of the fibrillar fibronectin extracellular matrix during gastrulation and neurulation in Xenopus laevis

“…In the MICRA system the FEL irradiation is perpendicular to the magnetic field, while for the Bruker system it is parallel to the field. A third FTICR‐FEL facility utilizes a free electron laser at the Science University of Tokyo (SUT) to irradiate ions in a commercial (Bruker) 4.7 T FTICR mass spectrometer (Fukui et al, 2006).…”

“…The Ohanessian group used the CLIO FEL and a Paul trap to obtain the IRMPD spectra of a 12‐residue fragment of stathmin in its phosphorylated and non‐phosphorylated forms, in conjunction with structural characterization of protonated phosphorylated serine, threonine, and tyrosine (Correia et al, 2008). Fukui and co‐workers at the Tokyo University of Science used the FEL‐SUT to study protonated substance P and protonated angiotensin II over the 5.7–9.5 µm wavelength range and observed mainly y/b‐type fragment ions (Fukui et al, 2006). Spectra of the largest system for which IRMPD spectra have been obtained to date, the 104 amino acid cytochrome c , showed clearly resolvable bands in the amide I and II spectral regions (Fig.…”

IR Spectroscopic Techniques to Study Isolated Biomolecules

“…Upon exiting the guide, the ions encounter the ICR cell at ground potential and slow down to a low kinetic energy (3 eV in this example), so that they can be efficiently captured in the cell. Figure adapted from Polfer et al [154] A.M. Rijs and J. Oomens [158]. Furthermore, the new IR FEL at the Fritz Haber Institute in Berlin has very recently been applied to obtain IR ion spectra [159].…”

Sequencing and characterization of oligosaccharides using infrared multiphoton dissociation and boronic acid derivatization in a quadrupole ion trap

“…Several studies have explored the use of IRMPD in an FTICR mass spectrometer for the analysis of oligosaccharides [16,[31][32][33][34][35]. For example, Lancaster et al compared the IRMPD spectra of O-linked and N-linked type oligosaccharides and found that cross-ring cleavages were observed only for the N-type oligosaccharides that are not readily fragmented by using CAD [16].…”

“…While the spectra were informative, poor signal-to-noise ratios often made spectral interpretation difficult [31]. Fukui et al used wavelength-tunable IRMPD in an FTICR mass spectrometer to determine the optimal dissociation wavelengths for sodium-cationized oligosaccharides [32]. While this technique is powerful, these types of lasers are not readily available.…”