Ion mobility mass spectrometry of IgG Fc glycopeptides from different subclasses

2014 Fiscal Year Final Research Report

• Project/Area Number: 24619014
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: オミクス計測科学
• Research Institution: Research Institute, Osaka Medical Center for Maternal and Child Health
• Principal Investigator: TAJIRI Michiko 地方独立行政法人大阪府立病院機構大阪府立母子保健総合医療センター(研究所), その他部局等, 流動研究員 (70581312)
• Co-Investigator(Renkei-kenkyūsha): HONGO Yayoi 独立行政法人理化学研究所, 連携支援ユニット, 専任技師 (40435681) ; NAKAMURA Takemichi 独立行政法人理化学研究所, 連携支援ユニット, 専任研究員 (10360611)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: 糖ペプチド / 糖タンパク質 / イオンモビリティー / 質量分析 / 衝突断面積 / 糖鎖－ペプチド間相互作用 / 免疫グロブリンG

Outline of Final Research Achievements

Glycosylation alters the physicochemical properties and biological activities of proteins. We analyzed glycopeptides using ion mobility mass spectrometry (IMS MS) and compared the data with the conformations calculated by molecular mechanics (MM) to investigate the interaction between protein and glycan in the vicinity of the attachment site.
In general, the collision cross sections (CCSs) of glycopeptides were smaller than those of peptides. Our findings from IMS MS and MM calculation suggested that the interaction between the innermost glycan and peptide backbone contributes to the compactness of glycopeptide ions in gas phase and the attachment of glycans gives a large influence on the conformation of peptide backbones independent of the glycan structures.

Free Research Field

質量分析学