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Evaluation Studies
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Dissociation of disulfide-intact somatostatin ions: the roles of ion type and dissociation method.
Rapid Communications in Mass Spectrometry : RCM 2009 September
The dissociation chemistry of somatostatin-14 was examined using various tandem mass spectrometry techniques including low-energy beam-type and ion trap collision-induced dissociation (CID) of protonated and deprotonated forms of the peptide, CID of peptide-gold complexes, and electron transfer dissociation (ETD) of cations. Most of the sequence of somatostatin-14 is present within a loop defined by the disulfide linkage between Cys-3 and Cys-14. The generation of readily interpretable sequence-related ions from within the loop requires the cleavage of at least one of the bonds of the disulfide linkage and the cleavage of one polypeptide backbone bond. CID of the protonated forms of somatostatin did not appear to give rise to an appreciable degree of dissociation of the disulfide linkage. Sequential fragmentation via multiple alternative pathways tended to generate very complex spectra. CID of the anions proceeded through CH(2)-S cleavages extensively but relatively few structurally diagnostic ions were generated. The incorporation of Au(I) into the molecule via ion/ion reactions followed by CID gave rise to many structurally relevant dissociation products, particularly for the [M+Au+H](2+) species. The products were generated by a combination of S-S bond cleavage and amide bond cleavage. ETD of the [M+3H](3+) ion generated rich sequence information, as did CID of the electron transfer products that did not fragment directly upon electron transfer. The electron transfer results suggest that both the S-S bond and an N-C(alpha) bond can be cleaved following a single electron transfer reaction.
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