2--3--4--trihydroxyflavone and jaceosidin

2--3--4--trihydroxyflavone has been researched along with jaceosidin* in 1 studies

Other Studies

1 other study(ies) available for 2--3--4--trihydroxyflavone and jaceosidin

Article	Year
Structure-activity relationships for flavone interactions with amyloid β reveal a novel anti-aggregatory and neuroprotective effect of 2',3',4'-trihydroxyflavone (2-D08). Bioorganic & medicinal chemistry, 2017, 07-15, Volume: 25, Issue:14 Naturally-occurring flavonoids have well documented anti-aggregatory and neuroprotective properties against the hallmark toxic protein in Alzheimer's disease, amyloid β (Aβ). However the extensive diversity of flavonoids has limited the insight into the precise structure-activity relationships that confer such bioactive properties against the Aβ protein. In the present study we have characterised the Aβ binding properties, anti-aggregatory and neuroprotective effects of a discreet set of flavones, including the recently described novel protein sumoylation inhibitor 2',3',4'-trihydroxyflavone (2-D08). Quercetin, transilitin, jaceosidin, nobiletin and 2-D08 were incubated with human Aβ Topics: Amyloid beta-Peptides; Animals; Benzothiazoles; Binding Sites; Cell Survival; Flavones; Flavonoids; Humans; Hydrogen Bonding; Microscopy, Electron, Transmission; Molecular Docking Simulation; Neuroprotective Agents; PC12 Cells; Peptide Fragments; Protein Binding; Protein Structure, Tertiary; Rats; Structure-Activity Relationship; Thiazoles	2017

Article

Year

Structure-activity relationships for flavone interactions with amyloid β reveal a novel anti-aggregatory and neuroprotective effect of 2',3',4'-trihydroxyflavone (2-D08).

Bioorganic & medicinal chemistry, 2017, 07-15, Volume: 25, Issue:14

Naturally-occurring flavonoids have well documented anti-aggregatory and neuroprotective properties against the hallmark toxic protein in Alzheimer's disease, amyloid β (Aβ). However the extensive diversity of flavonoids has limited the insight into the precise structure-activity relationships that confer such bioactive properties against the Aβ protein. In the present study we have characterised the Aβ binding properties, anti-aggregatory and neuroprotective effects of a discreet set of flavones, including the recently described novel protein sumoylation inhibitor 2',3',4'-trihydroxyflavone (2-D08). Quercetin, transilitin, jaceosidin, nobiletin and 2-D08 were incubated with human Aβ

Topics: Amyloid beta-Peptides; Animals; Benzothiazoles; Binding Sites; Cell Survival; Flavones; Flavonoids; Humans; Hydrogen Bonding; Microscopy, Electron, Transmission; Molecular Docking Simulation; Neuroprotective Agents; PC12 Cells; Peptide Fragments; Protein Binding; Protein Structure, Tertiary; Rats; Structure-Activity Relationship; Thiazoles

2017