Tyrosine Based Electrochemical Analysis of Amyloid-β Fragment (1-16) Binding to Metal(II) Ionsстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
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Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 14 ноября 2016 г.
Авторы:
Suprun Elena V.,
Zaryanov Nikolay V.,
Radko Sergey P.,
Kulikova Alexandra A.,
Kozin Sergey A.,
Makarov Alexander A.,
Archakov Alexander I.,
Shumyantseva Victoria V.
Аннотация:Electrochemical oxidation of the synthetic peptide Aβ(1–16), representing the metal-binding domain of Alzheimer’s human amyloid-β peptide, was investigated on carbon screen printed electrodes. The electrochemical behavior of Aβ(1–16), determined by the oxidation of the single Tyr-10 residue, was compared with that of free Tyr and with Tyr-lacking rat Aβ(1–16). The Aβ(1–16) oxidation signal detected at the potential of about 0.6 V (vs. Ag/AgCl) was used for monitoring peptide interactions with metal ions. For this purpose, four vitally important metal ions (Zn(II), Cu(II), Mg(II), and Ca(II)) were tested with respect to their binding to Aβ(1–16) within a wide range of ion concentrations in Tris-buffers with pH values from 5 to 9. Addition of both Zn(II) and Cu(II) ions significantly reduced the intensity of the Aβ(1–16) oxidation signal and shifted the peak to more positive potentials, while Mg(II) and Ca(II) ions had no noticeable effect. The results of electrochemical analysis of the metal(II)-Aβ(1–16) complexes were in good agreement with the literature data obtained by other methods. The proposed electrochemical assay based on the direct oxidation signal of a Tyr residue appears to be very promising for monitoring the metal-induced conformational changes of amyloid-β peptides in vitro as well as for studying other metal ion-protein complexes.