STRUCTURES OF B-PRODUCT AND A-PRODUCT IONS FROM THE FRAGMENTATION OF ARGENTINATED PEPTIDES

Citation
Vwm. Lee et al., STRUCTURES OF B-PRODUCT AND A-PRODUCT IONS FROM THE FRAGMENTATION OF ARGENTINATED PEPTIDES, Journal of the American Chemical Society, 120(29), 1998, pp. 7302-7309
Citations number
43
Categorie Soggetti
Chemistry
ISSN journal
00027863
Volume
120
Issue
29
Year of publication
1998
Pages
7302 - 7309
Database
ISI
SICI code
0002-7863(1998)120:29<7302:SOBAAI>2.0.ZU;2-#
Abstract
Argentinated (silver-containing) oligopeptides fragment under low-ener gy collision: conditions to yield abundant argentinated product ions. The structures of the [b(2) - H + Ag](+) and [a(2) - H + Ag](+) ions h ave been determined by means of tandem mass spectrometry and confirmed by comparison with synthesized derivatives df the candidate [b(2) - H + Ag](+) ion structure. The [b(2) - H + Ag](+) ion was found to be an N-argentinated oxazolone, which could subsequently form the [a(2) - H + Ag](+) ion and other product ions after collision activation. Tripe ptides containing proline as their second residue were observed to for m a relatively less abundant [b(2) - H + Ag](+) ion, which was postula ted to be an argentinated ketene.