General description

A cell-permeable 4,5-dianilinophthalimide that antagonizes Aβ42 amyloidogenesis as well as yeast Sup35 N-terminal domain- (aa 1 -124; NM) mediated prionogenesis by blocking the de novo fibrillization process and disassembling preformed NM fibers. Treatment with DAPH-12 greatly reduces the ratio between prion-harboring ([PSI⁺]) and non-prion-harboring ([psi^-]) yeast populations. DAPH-12 is also shown to effectively convert the [PSI⁺] phenotype into that of [psi^-] in a dose-dependent manner, while exhibiting no activity against [RNQ⁺] prion-containing cells. While DAPH-12 is in general more effective than EGCG (Cat. No. 324880) in antagonizing the various forms of NM prions both in cell-free and cell-based system, these two reagents used in tandem can create a synergistic effect against antiprion activity.

A cell-permeable 4,5-dianilinophthalimide that antagonizes Aβ42 amyloidogenesis as well as yeast Sup35 N-terminal domain- (aa 1 -124; NM) mediated prionogenesis by blocking the de novo fibrillization process and disassembling preformed NM fibers. Treatment with DAPH-12 greatly reduces the ratio between prion-harboring ([PSI⁺]) and non-prion-harboring ([psi^-]) yeast populations. DAPH-12 is also shown to effectively convert the [PSI⁺] phenotype into that of [psi^-] in a dose-dependent manner, while exhibiting no activity against [RNQ⁺] prion-containing cells. While DAPH-12 is in general more effective than EGCG (Cat. No. 324880) in antagonizing the various forms of NM prions both in cell-free and cell-based system, these two reagents used in tandem can create a synergistic effect against antiprion activity.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Other Notes

Roberts, B.E., et al. 2009. Nat. Chem. Bio.5, 936.Wang, H., et al. 2008. Proc. Natl. Acad. Sci. USA105, 7159.

Warning

Toxicity: Standard Handling (A)