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Selective cleavage enhanced by acetylating the side chain of lysine
Authors:Leixiaomeng Fu  Tingting Chen  Gaiqing Xue  Lily Zu  Weihai Fang
Institution:Beijing Normal University, , Beijing, 100875 P. R., China
Abstract:Selective cleavage is of great interest in mass spectrometry studies as it can help sequence identification by promoting simple fragmentation pattern of peptides and proteins. In this work, the collision‐induced dissociation of peptides containing internal lysine and acetylated lysine residues were studied. The experimental and computational results revealed that multiple fragmentation pathways coexisted when the lysine residue was two amino acid residues away from N‐terminal of the peptide. After acetylation of the lysine side‐chain, urn:x-wiley:10765174:media:jms3136:jms3136-math-0001 ions were the most abundant primary fragment products and the Lys(Ac)–Gly amide bond became the dominant cleavage site via an oxazolone pathway. Acetylating the side‐chain of lysine promoted the selective cleavage of Lys–Xxx amide bond and generated much more information of the peptide backbone sequence. The results re‐evaluate the selective cleavage due to the lysine basic side‐chain and provide information for studying the post‐translational modification of proteins and other bio‐molecules containing Lys residues. Copyright © 2013 John Wiley & Sons, Ltd.
Keywords:selective cleavage  lysine  acetylation  fragmentation mechanism  ESI MS/MS mass spectrometry
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