Negative ion fragmentations of deprotonated peptides. The unusual case of isoAsp: a joint experimental and theoretical study. Comparison with positive ion cleavages

H J Andreazza; Tianfang Wang; C J Bagley; P Hoffmann; J H Bowie

doi:10.1002/rcm.4107

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Negative ion fragmentations of deprotonated peptides. The unusual case of isoAsp: a joint experimental and theoretical study. Comparison with positive ion cleavages

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Negative ion fragmentations of deprotonated peptides. The unusual case of isoAsp: a joint experimental and theoretical study. Comparison with positive ion cleavages

H J Andreazza, Tianfang Wang, C J Bagley, P Hoffmann and J H Bowie

Rapid Communications in Mass Spectrometry, Vol.23(13), pp.1993-2002

2009

DOI: https://doi.org/10.1002/rcm.4107

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Abstract

The following peptides have been examined in this study: GLDFG(OH), caeridin 1.1 [GLLDGLLGLGGL(NH2)], 11 Ala citropin 1.1 [GLFDVIKKVAAVIGGL(NH2)], Crinia angiotensin [APGDRIYVHPF(OH)] and their isoAsp isomers. It is not possible to differentiate between Asp- and isoAsp-containing peptides (used in this study) using negative ion electrospray mass spectrometry. This is because the isoAsp residue cleaves to give the same fragment anions as those formed by δ and γ backbone cleavage of Asp. The isoAsp fragmentations are as follows: RNHCH(CO2H)-CHCONHRâ€² â†’ [RNH-(HO2CCHCHCONHRâ€²)] â†’ RNH-+HO2CCHCHCONHRâ€² and RNHCH(CO2H)-CHCONHRâ€² â†’ [RNH-(HO2CCHCHCONHRâ€²] â†’ -O2CCHCHCONHRâ€²+RNH2. Calculations at the HF/6-31+G(d)//AM1 level of theory indicate that the first of these isoAsp cleavage processes is endothermic (by +115 kJ mol-1), while the second is exothermic (-85 kJ mol-1). The barrier to the highest transition state is 42 kJ mol-1. No diagnostic cleavage cations were observed in the electrospray mass spectra of the MH+ ion of the Asp- and isoAsp-containing peptides (used in this study) to allow differentiation between these two amino acid residues.

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Title: Negative ion fragmentations of deprotonated peptides. The unusual case of isoAsp: a joint experimental and theoretical study. Comparison with positive ion cleavages
Authors: H J Andreazza (Author) - University of Adelaide
Tianfang Wang (Author) - University of Adelaide
C J Bagley (Author) - University of Adelaide
P Hoffmann (Author) - University of Adelaide
J H Bowie (Author) - University of Adelaide
Publication details: Rapid Communications in Mass Spectrometry, Vol.23(13), pp.1993-2002
Publisher: John Wiley & Sons Ltd.
Date published: 2009
DOI: 10.1002/rcm.4107
ISSN: 0951-4198
Organisation Unit: School of Science and Engineering - Legacy; University of the Sunshine Coast, Queensland; School of Science, Technology and Engineering; Centre for Bioinnovation
Language: English
Record Identifier: 99450498502621
Output Type: Journal article

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Collaboration types: Domestic collaboration
Web Of Science research areas: Biochemical Research Methods; Chemistry, Analytical; Spectroscopy

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