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https://www.selleckchem.com/products/i-138.html Consequently, the electron mobility is enhanced. At a 4% tensile strain, the electron mobility can reach up to 8000 cm2 V-1 s-1 at room temperature while the thermal conductivity is almost unaffected, yielding a state-of-the-art ZT value of 0.94 and 2.03 in n-type monolayer α-Te at 300 and 700 K, respectively. For completeness, the thermoelectric study of p-type monolayer α-Te is also conducted. These results beckon further experiments toward high-performance α-Te-based thermoelectric materials via doping, alloying, and compositing.The aggregation of neurotoxic amyloid-β (Aβ) polypeptides into aberrant extracellular senile plaques is the major neuropathological hallmark of Alzheimer's disease (AD). Inhibiting aggregation of these peptides to control the progression of this deadly disease can serve as a viable therapeutic option. In the current work, inherently fluorescent theranostic dopamine-tryptophan nanocomposites (DTNPs) were developed and investigated for their amyloid inhibition propensity along with their ability to act as a cellular bioimaging agent in neuronal cells. The antiaggregation potency of the nanocomposites was further investigated against an in vitro established reductionist amyloid aggregation model consisting of a mere dipeptide, phenylalanine-phenylalanine (FF). As opposed to large peptide/protein-derived robust and high-molecular-weight amyloid aggregation models of Alzheimer's disease, our dipeptide-based amyloid model provides an edge over others in terms of the ease of handling, synthesis, and cost-effectiveness. Results demonstrated positive antiaggregation behavior of the DTNPs toward both FF-derived amyloid fibrils and preformed Aβ-peptide fibers by means of electron microscopic and circular dichroism-based studies. Our results further pointed toward the neuroprotective effects of the DTNPs in neuroblastoma cells against FF amyloid fibril-induced toxicity and also that they significantly s

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