6533b820fe1ef96bd127a433
RESEARCH PRODUCT
Uncapping the N-terminus of a ubiquitous His-tag peptide enhances its Cu2+ binding affinity
J Swiątek-kozłowskaRobert WieczorekHenryk KozłowskiHenryk KozlowskiAleksandra HecelMagdalena Rowinska-zyrekJoanna Wątłysubject
inorganic chemicals010405 organic chemistryStereochemistryChemistryPeptide sequence tagVenom010402 general chemistry01 natural sciences0104 chemical sciencesInorganic ChemistryMetalN-terminuschemistry.chemical_compoundAcetylationvisual_artvisual_art.visual_art_mediumImidazoleBinding siteUncappingdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2019-01-01 | Dalton Transactions |