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dc.contributorWichita State University. Department of Chemistryen_US
dc.contributor.authorAnbalagan, Victoren_US
dc.contributor.authorPerera, B. A.en_US
dc.contributor.authorSilva, A. T. M.en_US
dc.contributor.authorGallardo, A. L.en_US
dc.contributor.authorBarber, M.en_US
dc.contributor.authorBarr, J. M.en_US
dc.contributor.authorTerkarli, S. M.en_US
dc.contributor.authorTalaty, Erach R.en_US
dc.contributor.authorVan Stipdonk, Michael J.en_US
dc.identifier.citationJournal of mass spectrometry : JMS. 2002 Sep; 37(9): 910-26.en_US
dc.descriptionClick on the DOI link below to access the article (may not be free).en_US
dc.description.abstractWe compared the tandem mass spectra of a range of native and acetylated Ag(+) cationized peptides to determine the influence of the derivatization step on the abundance of the [b(n) + 17 + Ag](+) product ions. Using tripeptides, the smallest for which the mechanisms to generate [b(2) - 1 + Ag](+) and [b(2) + 17 + Ag](+) products are both operative, we found that in most cases acetylation causes an increase in the abundance of the C-terminal rearrangement ion, [b(2) + 17 + Ag](+), relative to the rival N-terminal rearrangement ion, [b(2) - 1 + Ag](+). The presence of a free amino group to bind to the metal ion significantly influences the relative abundances of the product ions. We propose a mechanism for the formation of the [b(n) + 17 + Ag](+) that is based on the formation of a five-membered oxazolidin-5-one and tetrahedral carbon intermediate that may collapse to a peptide upon release of CO and an imine, aided by the fact that the ring formed during C-terminal rearrangement is both a hemiacylal and hemiaminal. We also identified an influence of amino acid sequence on the relative abundances of the [b(n) + 17 + Ag](+) and [b(n) - 1 + Ag](+) product ions, whereby bulky substituents located on the alpha-carbon of the amino acid to the C-terminal side of the cleavage site apparently promote the formation of the [b(n) + 17 + Ag](+) product over [b(n) - 1 + Ag](+) when the amino acid to the N-terminal side of the cleavage site is glycine. The latter ion is the favored product, however, when the bulky group is positioned on the alpha-carbon of the amino acid to the N-terminal side of the cleavage site.en_US
dc.publisherJohn Wiley and Sonsen_US
dc.relation.ispartofseriesJournal of mass spectrometry : JMSen_US
dc.relation.ispartofseriesJ Mass Spectromen_US
dc.titleFormation of [b(n) + 17 + Ag]+ product ions from Ag+ cationized native and acetylated peptidesen_US
dc.description.versionpeer revieweden_US
dc.rights.holderCopyright © 2002 John Wiley & Sons, Ltd.en_US

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