NDLI: Participation of C-H Protons in the Dissociation of a Proton Deficient Dipeptide

Content Provider	Springer Nature Link
Author	Koirala, Damodar Mistry, Sabyasachy Wenthold, Paul G.
Copyright Year	2017
Abstract	The dissociation of anionic dipeptides PheGly and GlyPhe, where Phe* refers to sulfonated phenyl alanine, has been investigated by using ion trap mass spectrometry. The dipeptides undergo collision-induced dissociation (CID) to give the same products, indicating that they rearrange to a common structure before dissociation. The rearrangement does not occur with the dipeptide methyl esters. The structures of the b$_{2}$ ions were investigated to determine the effect that having a remote, anionic site has on product formation. Comparison with the CID spectra for authentic structures shows that the b$_{2}$ ion obtained from GlyPhe* has predominantly a diketopiperazine structure. The CID spectra for the PheGly b$_{2}$ ion and the authentic oxazolone are similar, but differences in intensity suggest a two-component mixture. Isotopic labeling studies are consistent with the formation of two products, with one resulting from loss of a non-mobile proton on the Gly α-carbon. The results are attributed to the formation of an oxazole and oxazolone enol product. Electronic structure calculations predict that the enol structure of the PheGly b$_{2}$ ion is lower in energy than the keto version due to intramolecular hydrogen bonding with the sulfonate group. Graphical Abstract ᅟ
Starting Page	1313
Ending Page	1323
Page Count	11
File Format	PDF
ISSN	10440305
Journal	Journal of The American Society for Mass Spectrometry
Volume Number	28
Issue Number	7
e-ISSN	18791123
Language	English
Publisher	Springer US
Publisher Date	2017-04-20
Publisher Institution	The American Society for Mass Spectrometry
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Dipeptide dissociation b2 Ions Charge remote fragmentation Canonical structures Diketopiperazine Oxazolone Analytical Chemistry Biotechnology Organic Chemistry Proteomics Bioinformatics
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Structural Biology

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