Sialorphin and its analog as ligands for copper(II) ions

被引：4
|
作者：
Kamysz, Elzbieta [1 ]
Kotynia, Aleksandra [2 ]
Czyznikowska, Zaneta [2 ]
Jaremko, Mariusz [3 ,4 ]
Jaremko, Lukasz [3 ]
Nowakowski, Michal [4 ,5 ]
Brasun, Justyna [2 ]
机构：
[1] Univ Gdansk, Fac Chem, PL-80952 Gdansk, Poland
[2] Wroclaw Med Univ, Dept Inorgan Chem, PL-50139 Wroclaw, Poland
[3] Max Planck Inst Biophys Chem, Dept NMR Based Struct Biol, D-37077 Gottingen, Germany
[4] Polish Acad Sci, Inst Biochem & Biophys, PL-02106 Warsaw, Poland
[5] Warsaw Univ, Fac Chem, PL-02093 Warsaw, Poland
来源：
POLYHEDRON | 2013年 / 55卷
关键词：
Sialorphin; Peptides; Copper(II) ion; Metal ions complexes; Synthesis; Potentiometry; Stability constants; UV-Vis; CD; NMR; Theoretical calculations; HISTIDINE-CONTAINING PEPTIDES; COMPLEXES; LHRH; RAT; PROLINE; BINDING; RESIDUE; ABILITY; ACID;
D O I：
10.1016/j.poly.2012.10.055
中图分类号：
O61 [无机化学];
学科分类号：
070301 ; 081704 ;
摘要：
In this study the sialorphin (Gln-His-Asn-Pro-Arg) and its analog (Glp-His-Asn-Pro-Arg) were analyzed in terms of metal binding ability. Both peptides were synthesized using the solid-phase method. The application of number analytical methods: potentiometry, spectroscopy (UV-Vis, CD, NMR) and mass spectrometry allowed for a detailed characterization of the coordination abilities of presented peptides. The analysis of the obtained results has shown that both peptides are able to form a series of complexes. However due to the presence of free N-terminal amino group the sialorphin is more effective in metal ion binding. Nevertheless, in basic conditions both peptides involve the amide nitrogen belonging to the side chain of Asn3 moiety and form 4N complex with square planar structure. This unusual ability has been confirmed by the results obtained from the NMR studies. (C) 2013 Elsevier Ltd. All rights reserved.
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收藏
页码：216 / 224
页数：9
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