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Uncapping the N-terminus of a ubiquitous His-tag peptide enhances its Cu2+ binding affinity.
Autorzy
Rok wydania
2019
Czasopismo
Numer woluminu
48
Strony
13567-13579
DOI
10.1039/c9dt01635j
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
Metal complexes with an N-terminally free and N-terminally acetylated polyhistidine region of Echis ocellatus venom, with an interesting His-rich motif present in numerous metal binding proteins from all kingdoms of life (DHDHDHHHHHHPGSSV-NH2 and Ac-DHDHDHHHHHHPGSSV-NH2) show the role of the free amino group in the thermodynamic enhancement of Cu2+, Ni2+ and Zn2+ binding. In the studied sequences, Cu2+ can be coordinated by different sets of imidazole rings, and a 3–10 helix is detected in close proximity of Cu2+ binding sites. The complexes are more stable than those with a typical His6-tag, despite a similar copper(II) coordination mode in both cases.
Adres publiczny
http://dx.doi.org/10.1039/c9dt01635j
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