ISSN:
1076-5174
Keywords:
Chemistry
;
Analytical Chemistry and Spectroscopy
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
,
Physics
Notes:
The backbone cleavages for three series of protonated N-benzoyl tripeptide ions were studied in a hybrid tandem mass spectrometer: (i) benzoyl-Gly-Gly-Xxx, where Xxx = Gly, Ala, Val, Leu, Ile, Phe, Tyr, Met, Glu, Pro and Trp, (ii) benzoyl-Gly-Xxx-Gly, where Xxx = Gly, Ala, Leu, Phe, Tyr, Met and Trp, and (iii) benzoyl-Xxx-Gly-Gly, where Xxx = Gly, Ala, Val, Leu, Ile, Phe, Tyr, Met, Pro and Trp. C-Terminal y-type ions and N-terminal a- and b-type ions were noted in all three cases. For benzoyl-Gly-Gly-Xxx, a linear relationship between log (y1/b2) and the proton affinity of the C-terminal amino acid substituents was found: as the proton affinity of the C-terminal residue increases, the fraction of y1 ion formation increases. A similar relationship was noted for the benzoyl-Xxx-Gly-Gly tripeptides between log (y2/b1) and the proton affinity of the N-terminal amino acid substituent: as the proton affinity of the N-terminal residue increases, the fraction of b1 ion formation increases. For the series benzoyl-Gly-Xxx-Gly, these relationships did not hold true. These observations point to similar reaction pathways throughout the benzoyl-Gly-Gly-Xxx series and also similar pathways throughout the benzoyl-Xxx-Gly-Gly, but pathways that are substituent dependent for benzoyl-Gly-Xxx-Gly. The increased correlation coefficients for benzoyl-Gly-Gly-Xxx and benzoyl-Xxx-Gly-Gly when compared with the free tripeptides, suggest that fewer interfering competitive reactions exist, as fewer possibilities for internal hydrogen bonding exist in the N-benzoyl derivatives versus the free compounds.
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/jms.1190300410
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