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https://hdl.handle.net/11147/5154
Title: | Protonated Dipeptide Losses From B 5 and B 4 Ions of Side Chain Hydroxyl Group Containing Pentapeptides |
Authors: | Atik, Ahmet Emin Yalçın, Talat |
Keywords: | Dipeptide loss Macrocyclization Peptide fragmentation Water migration Ions |
Publisher: | American Chemical Society |
Source: | Atik, A.E., and Yalçın, T. (2013). Protonated dipeptide losses from b 5 and b 4 ions of side chain hydroxyl group containing pentapeptides. Journal of the American Society for Mass Spectrometry, 24(10). 1543-1554. doi:10.1007/s13361-013-0694-x |
Abstract: | In this study, C-terminal protonated dipeptide eliminations were reported for both b 5 and b 4 ions of side chain hydroxyl group (-OH) containing pentapeptides. The study utilized the model C-terminal amidated pentapeptides having sequences of XGGFL and AXVYI, where X represents serine (S), threonine (T), glutamic acid (E), aspartic acid (D), or tyrosine (Y) residue. Upon low-energy collision-induced dissociation (CID) of XGGFL (where X = S, T, E, D, and Y) model peptide series, the ions at m/z 279 and 223 were observed as common fragments in all b 5 and b 4 ion (except b 4 ion of YGGFL) mass spectra, respectively. By contrast, peptides, namely SMeGGFL-NH2 and EOMeGGFL- NH2, did not show either the ion at m/z 279 or the ion at m/z 223. It is shown that the side chain hydroxyl group is required for the possible mechanism to take place that furnishes the protonated dipeptide loss from b 5 and b 4 ions. In addition, the ions at m/z 295 and 281 were detected as common fragments in all b 5 and b 4 ion (except b 4 ion of AYVYI) mass spectra, respectively, for AXVYI model peptide series. The MS4 experiments exhibited that the fragment ions at m/z 279, 223, 295, and 281 entirely reflect the same fragmentation behavior of [M + H]+ ion generated from commercial dipeptides FL-OH, GF-OH, YI-OH, and VY-OH. These novel eliminations reported here for b 5 and b 4 ions can be useful in assigning the correct and reliable peptide sequences for high-throughput proteomic studies. [Figure not available: see fulltext.] |
URI: | https://doi.org/10.1007/s13361-013-0694-x http://hdl.handle.net/11147/5154 |
ISSN: | 1044-0305 1879-1123 1044-0305 |
Appears in Collections: | Chemistry / Kimya PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection |
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