FOOD SCIENCE ›› 2013, Vol. 34 ›› Issue (23): 47-50.doi: 10.7506/spkx1002-6630-201323011

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Analysis of Glycated Peptides by Neutral-loss-triggered CID MS3 Spectrometry

WANG Hui1,TU Zong-cai1,2,*,LIU Guang-xian3,SHA Xiao-mei1,XIAO Hui4   

  1. 1. State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China;
    2. College of Life Sciences, Jiangxi Normal University, Nanchang 330022, China;3. Jiangxi Academy of Agricultural Sciences,
    Nanchang 330200, China;4. Albert Einstein College of Medicine, Yeshiva University, New York 10461, USA
  • Received:2013-04-09 Revised:2013-11-13 Online:2013-12-15 Published:2014-01-03
  • Contact: tuzongcai zong-caiTU E-mail:tuzc_mail@yahoo.com.cn

Abstract:

Identification of the glycated sites in proteins plays an important role in the field of protein glycation. In the
present study, we have established a CID neutral-loss-triggered MS3 method to analyze the glycated sites in proteins. ESICID-
MS was used to stimulate multi-site cleavage in glycated Amadori peptides. MS3 scans triggered by neutral losses of
3H2O and 3H2O + HCHO produced similar results in terms of glycated peptide identification. However, neutral loss of 3H2O
resulted in more accurate glycated peptide identification in multi-stage activation experiments. The results showed that the
K227 was more easily glycated by D-glucose when compared with the K229 in ovalbumin under dry heating conditions.
Overall, the multi-stage activation approach could identify the glycation site in peptides with one glycosylation site.

Key words: glycated peptide, neutral-loss, collision-induced dissociation (CID), multi-stage MS

CLC Number: