A novel mass spectrometric method has been developed for obtaining sequence information on small peptides. The peptides are desorbed as intact neutral molecules into a Fourier transform ion cyclotron resonance mass spectrometer (FT-ICR) by means of laser-induced acoustic desorption (LIAD). Reactions of the neutral peptides with the dimethoxyphosphenium ion, P(OCH3)2+, occur predominantly by addition of the peptide to P(OCH3)2+ followed by the loss of two methanol molecules, thus yielding product ions with the composition (peptide + P - 2H)+. Upon sustained off-resonance irradiation for collision-activated dissociation (SORI-CAD), the (peptide + P - 2H)+ ions undergo successive losses of CO and NH{double bond, short}CHR or H2O, CO, and NH{double bond, short}CHR to yield sequence-related fragment ions in addition to the regular an- and bn-type ions. Under the same conditions, SORI-CAD of the analogous protonated peptides predominantly yields the regular an- and bn-type ions. The mechanisms of the reactions of peptides with P(OCH3)2+ and the dissociation of the (peptide + P - 2H)+ ions were examined by using model peptides and molecular orbital calculations. © 2007 American Society for Mass Spectrometry.
CITATION STYLE
Somuramasami, J., & Kenttämaa, H. I. (2007). Evaluation of a Novel Approach for Peptide Sequencing: Laser-induced Acoustic Desorption Combined with P(OCH3)2+ Chemical Ionization and Collision-activated Dissociation in a Fourier Transform Ion Cyclotron Resonance Mass Spectrometer. Journal of the American Society for Mass Spectrometry, 18(3), 525–540. https://doi.org/10.1016/j.jasms.2006.10.009
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