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Inne
Novel short-chain analogues of somatostatin as ligands for Cu(II) ions. Role of the metal ion binding on the spatial structure of the ligand.
Autorzy
Rok wydania
2012
Czasopismo
Journal of Inorganic Biochemistry
Numer woluminu
117
Strony
10-17
DOI
10.1016/j.jinorgbio.2012.08.023
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
In this paper we present the studies on coordination abilities of two short-chain analogues of somatostatin with free N-terminal and protected amino group towards copper (II) ions. The octreotide is the most popular analogue of the somatostatin (peptide hormone) used in medicine. Somatostatin analogues are used in diagnosis and treatment of the neuroendocrine tumors. Both analyzed analogues are characterized by the presence of two His instead of Cys residues in characteristic fragment of native peptide. We characterize coordination abilities of the ligands using potentiometric and spectroscopic methods. His-analogues of somatostatin are effective ligands for copper (II) ions. Both peptides are able to form the complexes with the cyclic structure.
Słowa kluczowe
Somatostatin, copper(II) complexes, histidine, Potentiometric measurements, spectroscopic studies, Coordination
Adres publiczny
http://dx.doi.org/10.1016/j.jinorgbio.2012.08.023
Strona internetowa wydawcy
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