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Poster Presentations
Day 4, June 25（Wed.）
Room P (Maesato East, Foyer, Ocean Wing)
- 4P-PM-04
ExD vs. EthCD: A Comparative Study for Top-Down Sequencing of Amphibian Disulfide Peptides
(1MSU-BIT, 2Agilent, 3Univ. Hong Kong)
oDmitrii Mazur1, Tatiana Samgina1, Yinan Li3, Michael Hare2, Yuriy Vasil'ev2, Albert Lebedev1
Since the last decades mass spectrometry (MS) has become a unique and the most common analytical tool for the sequence elucidation of proteins/peptides and detection of their post-translational modifications. The top-down strategy for sequencing implies analysis of intact peptide/protein infused directly into the mass spectrometer after preliminary separation by suitable separation technique. Application of a wide range of modern fragmentation tools (CID, HCD, IRMPD, UVPD, ETD, ECD) leads to sequencing of the target peptide/protein. Amphibians, particularly frogs, being under the stress release a cocktail of bioactive peptides, often found in their skin secretions. These peptides exhibit a wide range of biological activities (antimicrobial, antiviral etc.) Many of secreted by Ranid frogs peptides possess a disulfide cycle at their C-terminus, which is stable during some of the MS fragmentation experiments. Earlier we have demonstrated that electron-transfer/higher-energy collision dissociation (EThcD) can solve almost all problems becoming the unique tool for sequencing the intact disulfide peptides. This study has revealed an alternative method (ExD) that maintained the ability to perform MS sequencing of disulfide peptides from amphibian skin secretions, without compromising performance. Comparison of EThcD and ExD techniques brought new insights in the success of sequencing the disulfide peptides.