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- W624293811 abstract "Modulation of protein self-assembly has been a powerful strategy for controlling and understanding amyloid protein aggregation. Most modulators of amyloid aggregation only involve simple inhibition or acceleration. Here we report a new multivalent molecular motif, the polyethylenimine-perphenazine (PEI-P) conjugate which has a dual acceleration-inhibition modulation effect on amyloid β (Aβ) aggregation. Dose dependent results from Thioflavin T fluorescence assays, circular dichroism, and atomic force microscopy show that PEI-P conjugates accelerate formation of Aβ prefibrillar intermediates and then inhibit Aβ fibrillation. Furthermore, compared to perphenazine alone, PEI-P conjugates exhibit an enhanced inhibitory effect due to multivalency. Cell viability assays indicate that the PEI-P conjugates reduce the cytotoxicity of Aβ aggregates in a dose-dependent manner. This new modulation strategy may shed light on controlling amyloid aggregation, which offers a general concept for designing new modulators." @default.
- W624293811 created "2016-06-24" @default.
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- W624293811 date "2015-06-17" @default.
- W624293811 modified "2023-10-02" @default.
- W624293811 title "Molecular Design for Dual Modulation Effect of Amyloid Protein Aggregation" @default.
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- W624293811 doi "https://doi.org/10.1021/jacs.5b01651" @default.
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