Repozytorium
Wyszukaj
Kolekcje
Inne
Exploring the reactions of β-amyloid (Aβ) peptide 1-28 with AlIII and FeIII ions.
Autorzy
Rok wydania
2011
Czasopismo
Numer woluminu
50
Strony
6865-6867
DOI
10.1021/ic201069v
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
The reactions of human β-amyloid peptide 1–28 (Aβ28) with AlIII and FeIII ions were investigated by 1H NMR and electrospray ionization mass spectrometry (ESI-MS) under pH conditions close to physiological ones. 1H NMR titrations, performed in the 5.3–8.0 pH range, revealed that no measurable amounts of Aβ28-AlIII or Aβ28-FeIII adducts are formed; such metal adducts could not be obtained even by changing a number of experimental conditions, e.g., temperature, buffer, nature of the salt, etc. These observations were later confirmed by ESI-MS. It is thus demonstrated that Aβ28, at physiological pH, is not able to form binary complexes with AlIII and FeIII ions of sufficient stability to compete with metal hydroxide precipitation. The biological implications of these findings are discussed in the frame of current literature.
Adres publiczny
https://doi.org/10.1021/ic201069v
Strona internetowa wydawcy
Podobne publikacje
Verdoheme reactivity. Remarkable paramagnetically shifted 1H NMR spectra of intermediates from the addition of hydroxide or methoxide with FeII and FeIII verdohemes.
Latos-Grażyński Lechosław, Wojaczyński Jacek, Koerner R., Johnson J., Balch Alan L.
NMR studies of the Zn2+ interactions with rat and human β-amyloid (1-28) peptides in water-micelle environment.
Gaggelli Elena, Janicka-Kłos Anna, Jankowska Elżbieta, Kozłowski Henryk, Migliorini Caterina, Molteni E., Valensin Daniela, Valensin Gianni, Wieczerzak E.
Magnetism and crystal structures of CuII MnII and CuII NiII ordered bimetallic chains.
Bieńko Alina, Kłak Julia, Mroziński Jerzy, Domagała S., Korybut-Daszkiewicz B., Woźniak Krzysztof