On the mechanism of electron-capture-induced dissociation of peptide dications from ¹⁵N-labeling and crown-ether complexation

¹⁵N-labeling of di- and tripeptides reveals that electron capture to doubly protonated peptides results almost exclusively in ammonia loss from the N-terminal end, which clearly shows that a significant fraction of electron capture occurs at this end. In accordance with this finding, the competing channel of N-C _α bond breakage leads to z ^+̇ ions and neutral c fragments after electron capture to small dications. In larger peptides that live long enough for internal proton exchanges to occur, C ⁺ ions are also formed and in some cases in dominant yield. Attachment of one or two crown ethers to ammonium groups is likely to reduce the probability of proton transfer, which enhances the formation of z ^+̇ relative to c ⁺. The total yield of z ^+̇ and C ⁺ is, however, more or less unchanged, which indicates that proton transfer or hydrogen transfer from a NH ₃ group to the amide group is not required for the N-C _α bond breakage.