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

Suprun, Elena V.; Radko, Sergey P.; Khmeleva, Svetlana A.; Mitkevich, Vladimir A.; Archakov, Alexander I.; Makarov, Alexander А.; Shumyantseva, Victoria V.

doi:10.1016/j.elecom.2016.12.009

Cited by 26 publications

(9 citation statements)

References 29 publications

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“…The electrochemical response of solutions of Aβ 4–16 , Cu II :Aβ 1–16 , and Cu II :Aβ 4–16 at near-neutral pH has allowed assignment of the Cu II to Cu III oxidation to an irreversible wave near 1.04 V . This process occurs at potentials near those for oxidation of uncoordinated residues Y (0.8–0.9 V), H (1.1–1.4 V), and M (1.5–1.7 V), − complicating the assignment of metal and ligand-based redox reactions. In general, the Cu II presence slightly shifts oxidation peaks to a more positive potential .…”

Section: Resultsmentioning

confidence: 99%

Structural Insight into Redox Dynamics of Copper Bound N-Truncated Amyloid-β Peptides from in Situ X-ray Absorption Spectroscopy

et al. 2018

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X-ray absorption spectroscopy of Cu amyloid-β peptide (Aβ) under in situ electrochemical control (XAS-EC) has allowed elucidation of the redox properties of Cu bound to truncated peptide forms. The Cu binding environment is significantly different for the Aβ and the N-truncated Aβ, Aβ, and Aβ (Aβ) peptides, where the N-truncated sequence (FRH) provides the high-affinity amino-terminal copper nickel (ATCUN) binding motif. Low temperature (ca. 10 K) XAS measurements show the adoption of identical Cu ATCUN-type binding sites (Cu) by the first three amino acids (FRH) and a longer-range interaction modeled as an oxygen donor ligand, most likely water, to give a tetragonal pyramid geometry in the Aβ peptides not previously reported. Both XAS-EC and EPR measurements show that Cu:Aβ can be reduced at mildly reducing potentials, similar to that of Cu:Aβ. Reduction of peptides lacking the HH residues, Cu:Aβ, require far more forcing conditions, with metallic copper the only metal-based reduction product. The observations suggest that reduction of Cu species at mild potentials is possible, although the rate of reduction is significantly enhanced by involvement of HH. XAS-EC analysis reveals that, following reduction, the peptide acts as a terdentate ligand to Cu (H, H together with the linking amide oxygen atom). Modeling of the EXAFS is most consistent with coordination of an additional water oxygen atom to give a quasi-tetrahedral geometry. XAS-EC analysis of oxidized Cu:Aβ gives structural parameters consistent with crystallographic data for a five-coordinate Cu complex and the Cu complex. The structural results suggest that Cu and the oxidation product are both accommodated in an ATCUN-like binding site.

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Section: Resultsmentioning

confidence: 99%

Structural Insight into Redox Dynamics of Copper Bound N-Truncated Amyloid-β Peptides from in Situ X-ray Absorption Spectroscopy

et al. 2018

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“…The G peak appeared at ∼1580 cm −1 corresponding to the C-C stretching of the first-order scattering of the sp2 carbon hybridization, while the D peak was at ∼1340 cm −1 , corresponding to the carbon defects originating from the sp3 carbon hybridization [38]. The I D /I G ratio usually indicates the extent of disorder in a material, hence changes in this intensity ratio may reflect the disorder introduced with the carbon material after each chemical change [39].…”

Section: Scanning Electron Microscopymentioning

confidence: 99%

Novel Electrochemical Molecularly Imprinted Polymer-Based Biosensor for Tau Protein Detection

2021

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A novel electrochemical biosensor based on a molecularly imprinted polymer (MIP) was developed for the impedimetric determination of Tau protein, a biomarker of Alzheimer’s disease (AD). Indeed, a recent correlation between AD symptoms and the presence of Tau proteins in their aggregated form made hyperphosphorylated Tau protein (Tangles) a promising biomarker for Alzheimer’s diagnosis. The MIP was directly assembled on a screen-printed carbon electrode (C-SPE) and prepared by electropolymerization of 3-aminophenol (AMP) in the presence of the protein template (p-Tau-441) using cyclic voltammetry. The p-Tau-441 protein bound to the polymeric backbone was digested by the action of the proteolytic activity of proteinase K in urea and then washed away to create vacant sites. The performances of the corresponding imprinted and non-imprinted electrodes were evaluated by electrochemical impedance spectroscopy. The detection limit of the MIP-based sensors was 0.02 pM in PBS buffer pH 5.6. Good selectivity and good results in serum samples were obtained with the developed platform. The biosensor described in this work is a potential tool for screening Tau protein on-site and an attractive complement to clinically established methodologies methods as it is easy to fabricate, has a short response time and is inexpensive.

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“…[8,9] Of all the amino acids present in the Aβ chain, only three are redox active: histidine (His, H), methionine (Met, M) and tyrosine (Tyr, Y). The changes in voltammetric behaviour related to peak position and current decrease of the peaks corresponding to the oxidation of tyrosine, histidine and methionine allow for investigation of fibrilisation mechanisms not only of full-length Aβ, like Aβ and Aβ but also shorter fragments (like Aβ (10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20), Aβ (12−28)) or mutants (e.g.…”

Section: Introductionmentioning

confidence: 99%

Redox behaviour of Cu-Aβ(4-16) complexes related to Alzheimer's Disease

Wiloch,

Linfield,

Baran

et al. 2024

Electrochimica Acta

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

Cited by 26 publications

References 29 publications

Structural Insight into Redox Dynamics of Copper Bound N-Truncated Amyloid-β Peptides from in Situ X-ray Absorption Spectroscopy

Structural Insight into Redox Dynamics of Copper Bound N-Truncated Amyloid-β Peptides from in Situ X-ray Absorption Spectroscopy

Novel Electrochemical Molecularly Imprinted Polymer-Based Biosensor for Tau Protein Detection

Redox behaviour of Cu-Aβ(4-16) complexes related to Alzheimer's Disease

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