Nitration of amyloid-β peptide (1–42) as a protective mechanism for the amyloid-β peptide (1–42) against copper ion toxicity

Add time:08/03/2019    Source:sciencedirect.com

It is known that copper ion (Cu(II)) binds to amyloid-β peptide (Aβ), induces Aβ oligomer formation and ultimately exacerbates Aβ-aggregation neurotoxicity in Alzheimer's disease (AD). It becomes interesting to know that how this chemical modification of Aβ would affect interaction of Aβ and Cu(II) and their roles in the development of AD. In this work, we investigated the interaction of Aβ1–42 nitration with the toxic Cu(II). It showed that Cu(II)induced Aβ1–42 nitration in the presence of nitrite and hydrogen peroxide. Circular dichroism studies also revealed significant conformational change of Aβ1–42 and Tyr10 nitrated amyloid-β peptide(1–42) (Aβ1–42NT) when interacting with Cu(II). Even though nitration did not alter the binding of Aβ1–42 to Cu(II) or the peroxidative activity of Aβ1–42-Cu(II) complex, nitration ameliorated the aggregation and neurotoxicity of Aβ1–42 induced by Cu(II), which was also further confirmed by the cell study. Given our previous findings that Aβ nitration dramatically inhibited its aggregation and thus reduced its toxicity, we speculated that nitration of Aβ1–42 altered its intermolecular interaction, which protected itself against the toxicity of Cu(II). Based on this hypothesis, we propose that nitration of Aβ1–42 may be an important protective mechanism for normal function of Aβ1–42 and deserves more attention in AD drug development.

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