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The analysis of the structural aspects of Cu(II) binding by cyclic His/Asp-analogues of somatostatin.
Autorzy
Rok wydania
2020
Czasopismo
International Journal of Peptide Research and Therapeutics
Numer woluminu
26
Strony
969-977
DOI
10.1007/s10989-019-09900-9
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
Two new somatostatin analogs with a characteristic part of the sequence in their structures, -c(Cys-Phe-Trp-Lys-Thr-Cys)-, were synthesized and analyzed in terms of their coordination abilities with copper(II) ions. Cyclic peptides analyzed in our previous work had histidine and aspartic acid moieties in their structures which were responsible for metal ion coordination. In analyzed molecules these amino acids are also present. Peptides Ac[D1,2,9,10]c(SST) and Ac[H1,2,9,10]c(SST) have four aspartic acid or four histidine moieties, respectively. Both peptides bind Cu(II) effectively. Due to similar structures and the possibility of comparing the obtained results with these for the two previously published, the coordination abilities of two new ligands are possible to propose. Moreover, the effectiveness of copper(II) ion binding by four cyclic His/Asp-analogues of somatostatin is also discussed here. The peptide with four histidine moieties is the most efficient among described ligands.
Słowa kluczowe
Somatostatin, Somatostatin analogues, Copper complexes, Potentiometric measurements, Spectroscopy
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Pełny tekst licencji: https://creativecommons.org/licenses/by/3.0/pl/legalcode
Adres publiczny
http://dx.doi.org/10.1007/s10989-019-09900-9
Strona internetowa wydawcy
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