Effective binding of copper(II) with the peptide acetyl-GYDVEK-amide, model of the globular domain N-terminal of somatic histone H1 variants

The interaction of Cu(II) ions with the peptide Ac-GYDVEK-amide (N and C-terminal protected), a well conserved sequence located at N-terminal of the globular domain of somatic histone H1 variants (H1.1–H1.5) was studied by means of potentiometry and spectroscopic techniques. In the absence of a histidine residue, the β-COOH of the aspartic acid becomes the primary binding site. Curiously, this weak binding can prevent Cu(II) precipitation and...