Summary
In Alzheimer's disease, neurons slowly degenerate due to the accumulation of misfolded amyloid β and tau proteins. In our research, we performed extended studies directed at amyloid β and tau aggregation inhibition using <i>in cellulo</i> (<i>Escherichia coli</i> model of protein aggregation), <i>in silico</i>, and <i>in vitro</i> kinetic studies. We tested our library of 1-benzylamino-2-hydroxyalkyl multifunctional anti-Alzheimer's agents and identified very potent dual aggregation inhibitors. Among the tested derivatives, we selected compound <b>18</b>, which exhibited a unique profile of biological activity. This compound was the most potent and balanced dual aggregation inhibitor (Aβ<sub>42</sub> inhibition (inh.) 80.0%, tau inh. 68.3% in 10 μM), with previously reported <i>in vitro</i
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