Repozytorium
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Inne
Competition between the albumin and three histidine fragment of amyloid precursor protein sites to bind Cu(II).
Autorzy
Rok wydania
2008
Czasopismo
Numer woluminu
27
Strony
1511-1516
DOI
10.1016/j.poly.2008.01.025
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
The aim of this work was to check experimentally the relationship between the five-nitrogen donor system {3 × Nimid, 2 × N−} seen e.g. in the peptide fragments of the cysteine-rich amyloid precursor protein (APP) region and the albumin-like {NH2, 2 × N−, Nimid} coordination site. The protected and unprotected octadecapeptides DAHQERMDVSETHLHWHT and Ac-DAHQERMDVSETHLHWHT-NH2 were synthesized and potentiometric and spectroscopic studies were performed. A comparison of both metal-binding sites that occur in both peptides clearly shows that in the unprotected ligand albumin-like binding is much more efficient than the three His site, although around pH 5 both sites have a comparable ability to bind the Cu(II) ion. However, a comparison of the protected and unprotected peptides with their metal binding sites clearly shows that the three His site is very efficient in binding Cu(II) although less effective than the albumin-like motif.
Adres publiczny
https://doi.org/10.1016/j.poly.2008.01.025