日程：2026年7月21日（火）～7月23日（木）
会場：熊本城ホール
Jose Castro-Perez, VP, Product Management, SCIEX
Prof. Tereza Kadava, Biomolecular Mass Spectrometry and Proteomics, Utrecht University
Prof. Anthony W Purcell, Monash Biomedicine Discovery Institute Monash University
日時：2026年7月21日（火）17:30 - 19:30
場所：熊本城ホール3F 第1会場（大会議室A1-2）およびホワイエ
詳細は、公式サイトをご覧ください。
講演2要旨
Most bottom-up proteomics workflows currently rely on collisional dissociation (CID). While this approach is efficient for tryptic and unmodified peptides,
it rarely provides full peptide sequence coverage, especially when analyzing post-translational modified (PTM) peptides or longer non-tryptic peptides.
Here, we demonstrate the advantages of the hybrid EAciD fragmentation scheme on ZenoTOF 7600 and 8600 systems for de novo antibody sequencing and PTM analysis. Our data show that hyperthermoacidic (HTA) protease digestion in combination with EAciD fragmentation provides reliable peptide sequence annotation. This, together with full antibody sequence coverage by multiple peptide reads, facilitates de novo antibody sequencing in a single LC-MS/MS run. The EAciD fragmentation scheme is equally advantageous for glycopeptide analysis. The short EAciD reaction times, together with the ability to fine-tune the fragmentation parameters, yield rich fragmentation spectra that cover both peptide backbone and glycan fragment ions. This enhances the assignment of complex glycopeptides while maintaining similar throughput as CID.
講演3要旨
Immunopeptidomics is central to antigen discovery, but confident peptide identification remains challenging due to low sample complexity, limited peptide abundance, non-tryptic sequences, labile modifications, and ambiguity in residue assignment. In this presentation, I will discuss how hybrid fragmentation strategies on the ZenoTOF platform can improve both the depth and confidence of immunopeptidome analysis. Using Electron Activation with Collision Induced Dissociation (ExCID) approaches, we demonstrate improved peptide-spectrum match scores, increased access to previously under-sampled regions of the immunopeptidome, and enhanced confidence in sequence assignment. This is particularly valuable for phosphoimmunopeptidomics, where preservation of labile phosphorylation events supports improved phosphosite localisation and discovery of antigenic peptides. Hybrid fragmentation also provides opportunities to address persistent challenges such as isoleucine/leucine ambiguity, strengthening interpretation of HLA-bound peptide repertoires. Finally, I will highlight the application of ZT scan DIA for accurate identification and quantification of antigenic peptides, enabling more reproducible and quantitative immunopeptidomics workflows. Together, these advances support a shift from simply increasing peptide identifications toward deeper, more confident, and more biologically informative antigen discovery.