Issue 47, 2022

Dual mode of voltammetric studies on Cu(ii) complexes of His2 peptides: phosphate and peptide sequence recognition

Abstract

Copper(II) complexes of peptides with a histidine residue at the second position (His2 peptides) provide a unique profile of electrochemical behavior, offering signals of both Cu(II) reduction and Cu(II) oxidation. Furthermore, their structures with vacant positions in the equatorial coordination plane could facilitate interactions with other biomolecules. In this work, we designed a library of His2 peptides based on the sequence of Aβ5–9 (RHDSG), an amyloid beta peptide derivative. The changes in the Aβ5–9 sequence highly affect the Cu(II) oxidation signals, altered further by anionic species. As a result, Cu(II) complexes of Arg1 peptides without Asp residues were chosen as the most promising peptide-based molecular receptors for phosphates. The voltammetric data on Cu(II) oxidation for binary Cu(II)–His2 peptide complexes and ternary Cu(II)–His2 peptide/phosphate systems were also tested for His2 peptide recognition. We achieved a highly promising identification of subtle modifications in the peptide sequence. Thus, we introduce voltammetric measurement as a potential novel tool for peptide sequence recognition.

Graphical abstract: Dual mode of voltammetric studies on Cu(ii) complexes of His2 peptides: phosphate and peptide sequence recognition

Supplementary files

Article information

Article type
Paper
Submitted
21 Sep 2022
Accepted
09 Nov 2022
First published
10 Nov 2022
This article is Open Access
Creative Commons BY license

Dalton Trans., 2022,51, 18143-18151

Dual mode of voltammetric studies on Cu(II) complexes of His2 peptides: phosphate and peptide sequence recognition

A. Tobolska, K. Głowacz, P. Ciosek-Skibińska, W. Bal, W. Wróblewski and N. E. Wezynfeld, Dalton Trans., 2022, 51, 18143 DOI: 10.1039/D2DT03078K

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