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Uncapping the N-terminus of a ubiquitous His-tag peptide enhances its Cu2+ binding affinity

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Abstract

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.

Graphical abstract: Uncapping the N-terminus of a ubiquitous His-tag peptide enhances its Cu2+ binding affinity

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Publication details

The article was received on 18 Apr 2019, accepted on 06 Jul 2019 and first published on 08 Jul 2019


Article type: Paper
DOI: 10.1039/C9DT01635J
Dalton Trans., 2019, Advance Article

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    Uncapping the N-terminus of a ubiquitous His-tag peptide enhances its Cu2+ binding affinity

    J. Wątły, A. Hecel, R. Wieczorek, J. Świątek-Kozłowska, H. Kozłowski and M. Rowińska-Żyrek, Dalton Trans., 2019, Advance Article , DOI: 10.1039/C9DT01635J

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