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

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-NH 2 and Ac-DHDHDHHHHHHPGSSV-NH 2 ) show the role of the free...

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Bibliographic Details
Published in:Dalton transactions : an international journal of inorganic chemistry 2019-09, Vol.48 (36), p.13567-13579
Main Authors: W t y, J, Hecel, A, Wieczorek, R, wi tek-Koz owska, J, Koz owski, H, Rowi ska- yrek, M
Format: Article
Language:English
Online Access:Get full text
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Summary: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-NH 2 and Ac-DHDHDHHHHHHPGSSV-NH 2 ) show the role of the free amino group in the thermodynamic enhancement of Cu 2+ , Ni 2+ and Zn 2+ binding. In the studied sequences, Cu 2+ can be coordinated by different sets of imidazole rings, and a 3-10 helix is detected in close proximity of Cu 2+ binding sites. The complexes are more stable than those with a typical His6-tag, despite a similar copper( ii ) coordination mode in both cases. Copper( ii ) complexes with the studied His-rich motif are polymorphic, exhibit a 3-10 helix, and are more stable than a His6-tag complex.
ISSN:1477-9226
1477-9234
DOI:10.1039/c9dt01635j