Please use this identifier to cite or link to this item: 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
1044-0305
1879-1123
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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