Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/5266
Title: The role of lysine ?-amine group on the macrocyclization of b ions
Authors: Atik, Ahmet Emin
Görgülü, Güvenç
Yalçın, Talat
Atik, Ahmet Emin
Görgülü, Güvenç
Yalçın, Talat
Izmir Institute of Technology. Chemistry
Keywords: Asparagine
Glutamine
Lysine side chain ε-amine group
Macrocyclization of b ions
N-terminal acetylation
Issue Date: Apr-2012
Publisher: Elsevier Ltd.
Source: Atik, A. E., Görgülü, G. and Yalçın, T. (2012). The role of lysine ε-amine group on the macrocyclization of b ions. International Journal of Mass Spectrometry, 316-318, 84-90. doi:10.1016/j.ijms.2011.12.008
Abstract: A study was carried out to examine if the amine (NH 2) group located on the side chains of lysine (K), glutamine (Q), or asparagine (N) residue has any effect on the macrocyclization of b ions even though the N-terminals of the peptides were acetylated. The work utilized the model peptides Ac-KYAGFLVG, Ac-QYAGFLV-NH 2, and Ac-NYAGFLV-NH 2. The CID mass spectra of b 7 ions originated from these three peptides exhibited that the macrocyclization still occurred for the lysine containing peptide in spite of the N-terminal of the peptide was acetylated, but was failed to be observed for glutamine and asparagine containing peptides. These current results reveal that the lysine side chain ε-amine group has been involved in the macrocyclization of the peptide b ions for the N-terminal acetylated peptides and consequently, non-direct sequence b ions were observed in the CID mass spectra. However, due to the amide group on the side chains of the glutamine and asparagine residues, the nucleophilicity of their groups greatly reduced; therefore the scrambling b ions were not detected in their b 7 ion CID mass spectra. In addition, the effect of the lysine position was also studied for series of six isomeric octapeptides such as, Ac-KYAGFLVG, Ac-YKAGFLVG, Ac-YAKGFLVG, Ac-YAGKFLVG, Ac-YAGFKLVG and Ac-YAGFLKVG in order to examine the relationship between the intensities of non-direct sequence b ions and the lysine position in the octapeptide series. The results clearly demonstrated that the most abundant non-direct sequence b ions were observed for the first position of lysine residue in the N-terminal acetylated octapeptide, however, when the lysine residue gets closer to the C-terminal position the relative intensities of the scrambled b ions were greatly decreased.
URI: http://dx.doi.org/10.1016/j.ijms.2011.12.008
http://hdl.handle.net/11147/5266
ISSN: 1387-3806
Appears in Collections:Chemistry / Kimya
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection

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