Hitachi has succesfully developed high-throughput electron capture dissociation in a Linear Ion Trap (QuECD) for the NanoFrontier eLD. The reaction speed of QuECD is similar to conventional high-throughput CID.
Conventional CID is a widely used technique that cleaves peptide bonds by collisionally exciting the internal energy the bonds with neutral gas molecules. CID has several disadvantages that arise from its collision process: (1) collisions cannot deliver sufficient energy to all the peptide bonds for larger peptides resulting in incomplete sequence information, and (2) many types of post-translational modifications are lost during the collision process and it makes the determination of the modification location complicated.
ECD is a completely different dissociation method. It reduces positive charges via electron capture and induces cleavage of multiply-protonated peptides and proteins. The utility of this dissociation technique has become widely recognized as a powerful tool for proteomics.
This charge reduction dissociation technique randomly cleaves N-Cα bonds of the peptide backbone regardless of the type of amino acid residues on the N and C terminal sides of each bond (except the N terminal side of Proline). The cleavage occurs without apparent thermal excitation of the vibrational and rotational states of the peptide backbone bonds.
This unique characteristic of ECD provides advantages for proteomics: (1) evenly distributed cleavage sites over the entire peptide backbone, even for large peptides and proteins, yielding confident matches and enabling the analysis of intact proteins, and (2) efficient analysis of post-translational modifications (PTM’ s) due to the preservation of the modifications on the peptides/proteins after cleavage, resulting in easier identification of the modification sites.
Contact us forfurther product information. For products and services outside North America, please
click here.