Subnanomolar determination of dopamine by electrochemical sensor based on AuNPs- MWCNTs and mannan-Os (VI) adducts

Electroactive adducts, comprising 3α,6α–mannan attached to the six-valent osmium complex with N,N,N´,N?-tetramethylenediamine (simply denoted, Man- Os (VI) tmen) was immobilized on the surface of graphite electrodes via a simple adsorption route and then covered with poly(sodium-4 styrene sulfonate) (PSS). Cyclic voltammograms of modified electrodes GE/Man-Os (VI) tmen showed a clear and well-resolved anodic peak for 1 mM of dopamine DA, ascorbate AA, and urate UA at the potential range of -50 to +350 mV vs. Ag|AgCl|(KClsat.) the sensor GE/Man-Os (VI) tmen/PSS was successfully used for sensitive and selective determination of DA in the presence of an excess concentration of AA and UA, 5 mM and 0.5 mM respectively, using differential pulse voltammetry. Under optimized conditions, the peak current densities were linear from 0.1 nM to 20 μM of DA with a sensitivity of 358 μA μΜ-1 and a detection limit LOD (3SD/slope) of 2.8 nM. Further modifying of the sensor using multiwall carbon nanotubes decorated with gold nanoparticles (AuNPs-MWCNTs) led to substantial improvement in its analytical characteristics. The linear response of the electrode modified GE/ AuNPs-MWCNT/Man-Os (VI) tmen to DA was spanned from 1 pM to 40 μM with a high sensitivity of 624.49 μA μΜ-1 and a LOD (3SD/slope) of 0.17 pM

Electrochemical sensing of 2D condensation in amyloid peptides

The interfacial behavior of the model amyloid peptide octamer YYKLVFFC (peptide 1) and two other amyloid peptides YEVHHQKLVFF (peptide 2) and KKLVFFA (peptide 3) at the metal queous solution interface was studied by voltammetric and constant current chronopotentiometric stripping (CPS). All three peptides are adsorbed in a wide potential range and exhibit different interfacial organizations depending on the electrode potential. At the least negative potentials, chemisorption of peptide 1 occurs through the formation of a metal sulfur bond. This bond is broken close to -0.6 V. The peptide undergoes self-association at more negative potentials, leading to the formation of a "pit" characteristic of a 2D condensed film. Under the same conditions the other peptides do not produce such a pit. Formation of the 2D condensed layer in peptide 1 is supported by the time, potential and temperature dependences of the interfacial capacity and it is shown that presence of the 2D layer is reflected by the peptide CPS signals due to the catalytic hydrogen evolution. The ability of peptide 1 to form the potential-dependent 2D condensed layer has been reported neither for any other peptide nor for any protein molecule. This ability might be related to the well-known oligomerization and aggregation of Alzheimer amyloid peptides. © 2013 Elsevier Ltd. All rights reserved.SCOPUS: ar.jSCOPUS: ar.jinfo:eu-repo/semantics/publishe