Tuning the Redox Properties of Copper(II) Complexes with Amyloid-β Peptides

Magdalena Wiloch , Urszula Wawrzyniak , Iwona Ufnalska , Arkadiusz Bonna , Wojciech Bal , Simon C. Drew , Wojciech Wróblewski

Abstract

Copper complexes of metal binding domains of synthesized amyloid-β peptides – Aβ(1-16) and N-truncated Aβ(4-16) containing a novel N-terminal FRH sequence, as well as its shorter mutants were characterized by cyclic voltammetry. The influence of the peptide sequence and peptide to copper molar ratio on the electrochemical properties of the obtained structures were studied and discussed. The reversibility of the studied redox processes in copper complexes with Aβ(4-x) derivatives was also investigated. The results indicate the crucial role of Tyr10 in the redox process of the Aβ(4-x) complex, including the removal of reversibility of the Cu(II)/Cu(III) redox couple.
Author Magdalena Wiloch ZMB
Magdalena Wiloch,,
- Department Of Microbioanalytics
, Urszula Wawrzyniak ZMB
Urszula Wawrzyniak,,
- Department Of Microbioanalytics
, Iwona Ufnalska ZMB
Iwona Ufnalska,,
- Department Of Microbioanalytics
, Arkadiusz Bonna
Arkadiusz Bonna,,
-
, Wojciech Bal
Wojciech Bal,,
-
, Simon C. Drew
Simon C. Drew,,
-
, Wojciech Wróblewski ZMB
Wojciech Wróblewski,,
- Department Of Microbioanalytics
Journal seriesJournal of the Electrochemical Society, ISSN 0013-4651
Issue year2016
Vol163
No13
PagesG196-G199
Publication size in sheets0.5
Keywords in Englishamyloid-β, ATCUN-motif, copper(II), complexes, tyrosine, voltammetry
DOIDOI:10.1149/2.0641613jes
URL http://jes.ecsdl.org/content/163/13/G196.abstract
Languageen angielski
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Score (nominal)40
ScoreMinisterial score = 40.0, 28-11-2017, ArticleFromJournal
Ministerial score (2013-2016) = 40.0, 28-11-2017, ArticleFromJournal
Publication indicators WoS Impact Factor: 2016 = 3.259 (2) - 2016=3.307 (5)
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* presented citation count is obtained through Internet information analysis and it is close to the number calculated by the Publish or Perish system.
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