NDLI: Elucidation of PEGylation site with a combined approach of in-source fragmentation and CID MS/MS

Content Provider	Springer Nature Link
Author	Lu, Xiaojun Gough, P. Clayton DeFelippis, Michael R. Huang, Lihua
Copyright Year	2010
Abstract	Poly(ethylene glycol) (PEG)ylation of peptides and proteins creates significant challenges for detailed structural characterization, such as PEG heterogeneity, site of addition and number of attached PEGylated moieties. Recently, we published a novel LC/MS methodology with a post-column addition of amines to obtain accurate masses of PEGylated peptides and proteins. The accurate masses can be used to assign the structures and number of attached PEGs [15], but the PEGylation site remains unclear in situations where multiple potential attachments are involved. Here, we present a methodology combining in-source fragmentation (ISF) with CID-MS/MS to elucidate the PEGylated sites in PEGylated products. All PEGylated samples, either prepared in acidic solution, or collected from a RP-HPLC stream, were first ionized via ISF to produce products containing small PEG fragment attachment, and then those fragment ions obtained were sequenced via CID MS/MS to deduce the PEGylation site. The methodology was successfully applied to PEGylated glucagon and IgG4 antibody light chain, which demonstrated that the small PEG fragments attached were stable during the CID activation.
Starting Page	810
Ending Page	818
Page Count	9
File Format	PDF
ISSN	10440305
Journal	Journal of The American Society for Mass Spectrometry
Volume Number	21
Issue Number	5
e-ISSN	18791123
Language	English
Publisher	Springer-Verlag
Publisher Date	2010-01-25
Publisher Institution	The American Society for Mass Spectrometry
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Analytical Chemistry Biotechnology Organic Chemistry Proteomics Bioinformatics
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Structural Biology

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