A Comparative Interaction between Copper Ions with Alzheimer'sβAmyloid Peptide and Human Serum Albumin

Abstract

The interaction of Cu2+with the first 16 residues of the Alzheimer's amyliodβpeptide,Aβ(1–16), and human serum albumin (HSA) were studied in vitro by isothermal titration calorimetry at pH 7.2 and 310 K in aqueous solution. The solvation parameters recovered from the extended solvation model indicate that HSA is involved in the transport of copper ion. Complexes betweenAβ(1–16) and copper ions have been proposed to be an aberrant interaction in the development of Alzheimer's disease, where Cu2+is involved inAβ(1–16) aggregation. The indexes of stability indicate that HSA removed Cu2+fromAβ(1–16), rapidly, decreased Cu-induced aggregation ofAβ(1–16), and reduced the toxicity ofAβ(1–16) + Cu2+significantly.