Copper(I) and copper(II) binding to β-amyloid 16 (Aβ16) studied by electrospray ionization mass spectrometry

Copper-b-amyloid 16 (Aβ16) complexes were investigated by electrospray ionization mass spectrometry (ESI-MS). Copper(I) and (II) complexes were formed on-line in a microchip electrospray emitter by using a sacrificial copper electrode as the anode in positive ionization mode. In the presence of ascorbic acid in the peptide solution, the amount of Cu(I)-Aβ16 generated electrochemically was even higher. A kinetic model is proposed to account for the generation of copper complexes. The structure of Cu(I)-Aβ16 was investigated by tandem mass spectrometry (MS/MS), and the binding site of Cu(I) to Aβ16 was identified at the His13, His14 residues. Cu(II)-Aβ16 was also investigated by MS/MS and, based on the unusual observations of a-ions, the two binding residues of His13 and His14 of Aβ16 to Cu(II) were also confirmed. This approach provides direct information on Cu(I)-Aβ16 complexes generated in solution from metallic copper and gives evidence that both His13 and His14 are involved in the coordination of both Cu(I)- and Cu(II)-Aβ16 complexes.

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Metallomics, 2, 474-479
Royal Society of Chemistry

 Record created 2010-08-10, last modified 2018-03-17

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