A Comparative Interaction between Copper Ions with Alzheimer's ß Amyloid Peptide and Human Serum Albumin.

The interaction of Cu(2+) with the first 16 residues of the Alzheimer's amyliod ß peptide, Aß(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 between Aß(1-16) and copper ions have been proposed to be an aberrant interaction in the development of Alzheimer's disease, where Cu(2+) is involved in Aß(1-16) aggregation. The indexes of stability indicate that HSA removed Cu(2+) from Aß(1-16), rapidly, decreased Cu-induced aggregation of Aß(1-16), and reduced the toxicity of Aß(1-16) + Cu(2+) significantly.