<p> A high-throughput screening was used to identify protein aggregation inhibitors in vitro and in cell culture. Compounds selected in the primary screens were validated in dilution series in order to identify compounds active at very low concentrations. Clustering of the compound hits subsequently revealed a consensus structure common to active protein aggregation inhibitors. This lead structure was further modified to optimize its medicinal-chemical properties. The resulting candidates strongly reduced scrapie prion proteins in cell culture at nanomolar concentrations. They also revealed high therapeutic potential in mice infected with scrapie prions. The same compounds also inhibit formation
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Flexible and rigid, heavy-metal free organic redox polymer batteries
09.03.2017 | TechnologieAllianz e.V.
Quat primer polymers the universal key to permanent surface functionalization
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The results will be published on March 22 in the journal „Astronomy & Astrophysics“.
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