日本質量分析学会 第66回質量分析総合討論会

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第4日 5月18日(金) 12:20~12:40 A会場(オービットホール)

High Efficient and Precise Glycoproteomic Analysis with Intelligent Technology

(1Fudan IBS2CAS Computing Tech)
oYang, Pengyuan1Cao, Weiqian1Liu, Mingqi1Zeng, Wenfeng2Liu, Chao2Fang, Pan1Shen, Huali1He, Simin2

Protein glycosylation is a heterogeneous post-translational modification that generates great proteomic diversity and gives rise to functional variance. High efficient and precise characterization of protein glycosylation at site-specific level and the proteome scale is critical for understanding the biological functions. To achieve this goal, we propose a series of identification strategies and searching engines: pGlyco1.0, pGlcyo2.0 and pGlyco3.0. pGlyco1.0 is a pipeline for the identification of intact glycopeptides by integrating HCD-MS/MS, CID-MS/MS and MS3, and using a novel target-decoy method to estimate the false discovery rate of the glycan identification. pGlyco2.0 is a one-step tandem MS strategy for intact glycopeptide identification with optimized stepped-energy fragmentation and a dedicated search engine. With pGlyco2.0, intact glycopeptides could be identified at proteome scale and with comprehensive quality control including false discovery rate evaluation at all three levels of matches to glycans, peptides and glycopeptides. In pGlyco3.0, a database-free algorithm was developed for universal glycoproteome analysis without user-defined glycan composition list or glycan structure database. A large-scale N-glycoproteome dataset containing more than 50,000 unique N-glycopeptides was established with these strategies. We are moving towards to universal O-glycoproteome analysis.