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- W4382022752 abstract "Interaction of amyloid-β peptides (Aβ), Aβ fragments, and mutated Aβ with Cu(II) was systematically investigated using cyclic voltammetry (CV) on boron-doped diamond electrode with outstanding electrochemical properties. When the same ratio of Aβ to Cu(II) was used, the depressed order of redox current (Aβ(1–42), Aβ(1–16), Aβ(Y–F) > Aβ(H–N) > Aβ(25–35)) was observed for redox activity. Judging by the results of CVs, the resulting mutant Aβ(H–N) showed little affinity with Cu(II) if histidines were mutated individually. The absorption decrease and fluorescence quenching of Aβ(H– N)-Cu(II) were unconspicuous and insensitive compared with that of Aβ(1–16)–Cu(II), further proving that electron structure of tyrosine was not directly attacked and degraded by Cu(II). Almost the same CVs between Aβ(1–16)–Cu(II) and Aβ(Y–F)(tyrosine→phenylalanine)–Cu(II) along with the absence of tyrosine characteristic peak in absorption and fluorescent spectra confirmed that tyrosine was not the potential O ligand. The unchanged redox signal of Aβ(1–16)–Cu(II) compared with Aβ(Y–F)– Cu(II), and the same result of the Aβ(1–42)–Cu(II) and Aβ(25–35)–Cu(II) even the exogenous methionine–Cu(II) clarified that the reduction of Cu(II) was not aroused by Tyr-10 or Met-35 directly" @default.
- W4382022752 created "2023-06-27" @default.
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- W4382022752 date "2012-04-01" @default.
- W4382022752 modified "2023-09-23" @default.
- W4382022752 title "Electrochemical Monitoring of the Interaction of Cu(II) with Amyloid-B Peptides on Boron-Doped Diamond Electrode" @default.
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- W4382022752 doi "https://doi.org/10.1016/s1452-3981(23)13937-x" @default.
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