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).

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)

MAMMI, STEFANO;PEGGION, EVARISTO
1983

Abstract

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).
1983
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11577/2520665
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