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Inne
The role of the βAsp residue in copper(II) binding by modified peptides.
Autorzy
Rok wydania
2012
Czasopismo
Numer woluminu
53
Strony
1652-1655
DOI
10.1016/j.tetlet.2012.01.087
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
The synthesis and binding abilities of peptides containing β-amino acids towards Cu(II) ions are presented. The peptides studied were: Ala-βAsp-Ser-Gly and Arg-Lys-βAsp-Val-Tyr. Potentiometric titrations were carried out to establish the stoichiometry of the resulting metal-ligand complexes. The copper(II) coordination mode of the complexes was investigated by performing detailed spectroscopic analyses (UV–Vis, CD) in strict correlation with potentiometric measurements. The results obtained on the β-peptides studied allowed the characterization of the influence of this structural modification on the coordination abilities of the peptides. Moreover, the role of the α-Asp position in the peptide chain was also described.
Słowa kluczowe
ß-Amino-acid, ß-Peptide, copper(II), complex
Adres publiczny
https://doi.org/10.1016/j.tetlet.2012.01.087
Strona internetowa wydawcy
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