Macromolecularization of a tripeptide analog of the Cu(II) binding site of human serum albumin. I. Synthesis, conformation, and binding properties of a Gly-Gly-His derivative of poly(L-lysine)

The side chain of poly(L-Lysine) was derivatized with the tripeptide Gly-Gly-His, a good imetic of the Cu(II) binding site of serum albumin. The aim was to obtain a macromolecular adduct with high affinity for Cu(II) ions. We describe the synthesis and the preliminary conformational properties of this adduct, which exhibits strong affinity toward Cu(II) and Ni(II).