Repozytorium

Copper(II) binding to Cap43 protein fragments.

Autorzy

Maria Antonietta Zoroddu

Teresa Kowalik-Jankowska

Serenella Medici

Massimiliano Peana

Henryk Kozłowski

Rok wydania

2008

Czasopismo

Dalton Transactions

Strony

6127-6134

DOI

10.1039/B808600A

Kolekcja

Naukowa

Język

Angielski

Typ publikacji

Artykuł

Streszczenie

The C-terminal 20 and 30 amino acid sequences of Cap43 protein were chosen as models to study their interactions with Cu(II) ions. The behaviour of the 20 amino acid Ac–TRSRSH6TSEG–TRSRSH16TSEG and 30 amino acid Ac–TRSRSH6TSEG–TRSRSH16TSEG–TRSRSH26TSEG peptides towards Cu(II) ions at different pH values and different ligand-to-metal molar ratios, was examined. Spectroscopic (EPR, UV-Vis) and potentiometric techniques were performed to understand the details of metal binding to the peptides. The study showed that, starting from pH 4.0, each 10 amino acid fragment T1R2S3R4S5H6T7S8E9G10 was able to independently coordinate a single Cu(II) ion. The coordination mode involved the imidazole nitrogen of histidine H6 residue, and three amidic nitrogens from histidine H6, serine S5, and arginine R4 residues, respectively.

Adres publiczny

DOI https://doi.org/10.1039/B808600A

Strona internetowa wydawcy

https://www.rsc.org/

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