Electrochemical oxidation of amyloid-beta peptide isoforms on carbon screen printed electrodes

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• 作者：Elena V. Suprun^a ; ^{lenasuprun@mail.ru} ; Sergey P. Radko^a ; ^b ; Svetlana A. Khmeleva^a ; ^b ; Vladimir A. Mitkevich^b ; Alexander I. Archakov^a ; Alexander A. Makarov^b ; Victoria V. Shumyantseva^a
• 关键词：Aggregation ; Amino acid residue ; Amyloid-β peptide (1&ndash ; 42) ; Mutant ; Oxidation
• 刊名：Electrochemistry Communications
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：75
• 期：Complete
• 页码：33-37
• 全文大小：975 K
• 卷排序：75

文摘

Aβ42 is oxidized via Tyr, His, and Met residues at carbon SPE. Aβ42 Met-35 residue oxidation produces a broad wave at about 1.2–1.5 V (vs. Ag/AgCl). Ser-8 phosphorylation affects the Aβ42 signal at about 1.2–1.5 V (vs. Ag/AgCl). Oxidation is sensitive to amino acid substitutions in the Aβ42 peptide, such as D7H. Upon the aggregation of Aβ42 and its isoforms, the Tyr, His, and Met oxidation signals decrease.