Repozytorium
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Kolekcje
Inne
Cu2+ and Ni2+ interactions with N-terminal fragments of Hpn and Hpn-like proteins from Helicobacter pylori : unusual impact of poly-Gln sequence on the complex stability.
Autorzy
Rok wydania
2011
Czasopismo
Journal of Inorganic Biochemistry
Numer woluminu
105
Strony
208-214
DOI
10.1016/j.jinorgbio.2010.11.004
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
The N-terminal protected and unprotected peptides MAHHEEQHG-NH2, Ac-MAHHEEQHG-NH2 from Hpn (Helicobacter histidine-rich protein) and MAHHEQQQQQQA-NH2, Ac-MAHHEQQQQQQA-NH2 from Hpn-like protein, respectively, were synthesized and their interactions with Cu2+ and Ni2+ ions were studied by potentiometric, UV–visible, CD, and EPR techniques. The studies have shown that because of their albumin-like sequence, unprotected peptides are very effective chelating agents for both studied metals. The presence of the hexa-glutamine sequence has very distinct impact on the stability of the complexes formed even if direct interactions with metal ions were not found. The much more effective Ni2+ binding by Hpn-like N-terminal domain when compared to Hpn protein could be critical for different biological functions played by both proteins.
Słowa kluczowe
Cu complexes, Ni complexes, Albumin-like binding, Metallopeptides
Adres publiczny
https://doi.org/10.1016/j.jinorgbio.2010.11.004
Strona internetowa wydawcy
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