Repozytorium
Wyszukaj
Kolekcje
Inne
The unusual coordination abilities of the peptides with βXaaHisGlyHis sequence. The influence of structural modification if the peptide chain on the copper(II) binding.
Autorzy
Rok wydania
2010
Czasopismo
Numer woluminu
39
Strony
6518-6523
DOI
10.1039/B923371G
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
The coordination abilities of tetrapeptides containing β-amino acids towards Cu(II) ions are presented. The studied tetrapeptides were: Ac-βAlaHisGlyHis, βAlaHisGlyHis, Ac-βAspHisGlyHis, βAspHisGlyHis, Ac-βAspHisGly-DHis and βAspHisGly-DHis. Thorough potentiometric titrations were carried out to establish the stoichiometry of the resulting metal–ligand complexes and the role of free -αCOO− side chain group in metal binding. The copper(II) coordination mode of the complexes was investigated by performing detailed spectroscopic analyses (UV-Vis, EPR, CD) in strict correlation with potentiometric measurements.
Adres publiczny
http://dx.doi.org/10.1039/B923371G
Strona internetowa wydawcy
Podobne publikacje
The role of the histidine residue in the coordination abilities of peptides with a multi-histidine sequence towards copper(II) ions.
Matera A., Brasuń Justyna, Cebrat Marek, Świątek-Kozłowska Jolanta
Influence of the modification of the cosmetic peptide Argireline on the affinity toward copper(II) ions
Wyrzykowski Dariusz, Wieczorek Robert, Kloska Anna, Errante Fosca, Papini Anna Maria, Makowska Joanna
The role of histidine residue in coordination abilities of peptides with multi hisidine sequence towards nickiel(II) ions.
Matera A., Brasuń Justyna, Cebrat Marek, Świątek-Kozłowska Jolanta