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References
Analysis of Tau-441 protein in clinical samples using rGO/AuNP nanocomposite-supported disposable impedimetric neuro-biosensing platform: Towards Alzheimer's disease detection
TALANTA
Authors: Karaboga, Munteha Nur Sonuc; Sezginturk, Mustafa Kemal
Changes in isoforms of Tau protein, which are critical for microtubule functioning, are accepted as being responsible for diseases characterized by dementia, in particular Alzheimer's disease (AD). In this comprehensive study, a single-use neuro-biosensing probe for the determination of Tau-441 protein was developed by utilizing the power of nanocomposites consisting of reduced graphene oxide (rGO) and gold nanoparticles (AuNP) using electrochemical impedance spectroscopy (EIS) and cyclic voltammetry (CV). The nanocomposite surface (rGO-AuNP) was modified with 11-mercaptoundecanoic acid (11-MUA) act as covalent anchorer to increase the sensitivity of the assay. Surface coverage value and pinhole ratio were calculated using EIS data. Kramers-kronig data, which helps to interpret instrumental errors, are also calculated. The immunoreaction of Tau-441 with anti-Tau was monitored simultaneously with Single Frequency Impedance (SFI). The changes in surface morphology were evaluated with scanning electron microscopy (SEM), atomic force microscopy (AFM) and Fourier transform infrared spectroscopy (FTIR). The designed immunosensor showed a linear response within the concentration range of 1-500 pg/mL for the target analyte Tau-441 and the limit of detection was found to be 0.091 pg/mL. The promising point of the study is that this neuro-biosensor system can capture the Tau-441 target protein in both serum fluid and cerebrospinal fluid (CSF) samples with recoveries ranging from 96% to 108%.
Anisotropic diffusion and traveling waves of toxic proteins in neurodegenerative diseases
PHYSICS LETTERS A
Authors: Kevrekidis, P. G.; Thompson, Travis B.; Goriely, Alain
Neurodegenerative diseases are closely associated with the amplification and invasion of toxic proteins. In particular Alzheimer's disease is characterized by the systematic progression of amyloid-p and t-proteins in the brain. These two protein families are coupled and it is believed that their joint presence greatly enhances the resulting damage. Here, we examine a class of coupled chemical kinetics models of healthy and toxic proteins in two spatial dimensions. The anisotropic diffusion expected to take place within the brain along axonal pathways is factored in the models and produces a filamentary, predominantly one-dimensional transmission. Nevertheless, the potential of the anisotropic models towards generating interactions taking advantage of the two-dimensional landscape is showcased. Finally, a reduction of the models into a simpler family of generalized Fisher-Kolmogorov-Petrovskii-Piskunov (FKPP) type systems is examined. It is seen that the latter captures well the qualitative propagation features, although it may somewhat underestimate the concentrations of the toxic proteins. (C) 2020 Elsevier B.V. All rights reserved.
COA
Publication 
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