lignans and Protein-Aggregation--Pathological

lignans has been researched along with Protein-Aggregation--Pathological* in 2 studies

Other Studies

2 other study(ies) available for lignans and Protein-Aggregation--Pathological

Article	Year
Effect of the Biphenyl Neolignan Honokiol on Aβ ACS chemical neuroscience, 2017, 09-20, Volume: 8, Issue:9 The biphenyl neolignan honokiol is a neuroprotectant which has been proposed as a treatment for central nervous system disorders such as Alzheimer's disease (AD). The death of cholinergic neurons in AD is attributed to multiple factors, including accumulation and fibrillation of amyloid beta peptide (Aβ) within the brain; metal ion toxicity; and oxidative stress. In this study, we used a transgenic Caenorhabditis elegans model expressing full length Aβ Topics: Amyloid beta-Peptides; Animals; Biphenyl Compounds; Caenorhabditis elegans; Catechin; Chelating Agents; Cholinesterase Inhibitors; Drug Stability; Free Radical Scavengers; Humans; Iron; Lignans; Molecular Docking Simulation; Molecular Structure; Neuroprotective Agents; Paralysis; Peptide Fragments; Picrates; Protein Aggregation, Pathological; Protein Multimerization; Resveratrol; Stilbenes	2017
Lignans from the root of Paeonia lactiflora and their anti-β-amyloid aggregation activities. Fitoterapia, 2015, Volume: 103 Four new neolignans (1-4), together with two known lignans (5 and 6), were isolated from the root of Paeonia lactiflora. Compounds 1 and 2 were two racemates and were separated by chiral high performance liquid chromatography (HPLC) to give all of the four stereoisomeric forms sharing a common planar structure. Compounds 3 and 4 were two neolignan glycoside diastereomers but interestingly appeared to be enantiomers: they had the extremely similar (1)H and (13)C NMR spectra and had to be solved only by chiral HPLC. Their structures were determined by spectroscopic analysis, including 1D and 2D NMR, HRESIMS and electronic circular dichroism experiments. All compounds were evaluated for their inhibitory effects on β-amyloid aggregation, and the optical pure compound 2b was found to show the optimal Aβ(1-42) aggregation inhibition potency (81.1% at 20 μM). In addition, despite large amount of chemical studies performed on genus Paeonia, the lignans were reported for the first time. Topics: Amyloid beta-Peptides; Lignans; Molecular Docking Simulation; Molecular Structure; Paeonia; Peptide Fragments; Plant Roots; Protein Aggregation, Pathological	2015

Article

Year

Effect of the Biphenyl Neolignan Honokiol on Aβ

ACS chemical neuroscience, 2017, 09-20, Volume: 8, Issue:9

The biphenyl neolignan honokiol is a neuroprotectant which has been proposed as a treatment for central nervous system disorders such as Alzheimer's disease (AD). The death of cholinergic neurons in AD is attributed to multiple factors, including accumulation and fibrillation of amyloid beta peptide (Aβ) within the brain; metal ion toxicity; and oxidative stress. In this study, we used a transgenic Caenorhabditis elegans model expressing full length Aβ

Topics: Amyloid beta-Peptides; Animals; Biphenyl Compounds; Caenorhabditis elegans; Catechin; Chelating Agents; Cholinesterase Inhibitors; Drug Stability; Free Radical Scavengers; Humans; Iron; Lignans; Molecular Docking Simulation; Molecular Structure; Neuroprotective Agents; Paralysis; Peptide Fragments; Picrates; Protein Aggregation, Pathological; Protein Multimerization; Resveratrol; Stilbenes

2017

Lignans from the root of Paeonia lactiflora and their anti-β-amyloid aggregation activities.

Fitoterapia, 2015, Volume: 103

Four new neolignans (1-4), together with two known lignans (5 and 6), were isolated from the root of Paeonia lactiflora. Compounds 1 and 2 were two racemates and were separated by chiral high performance liquid chromatography (HPLC) to give all of the four stereoisomeric forms sharing a common planar structure. Compounds 3 and 4 were two neolignan glycoside diastereomers but interestingly appeared to be enantiomers: they had the extremely similar (1)H and (13)C NMR spectra and had to be solved only by chiral HPLC. Their structures were determined by spectroscopic analysis, including 1D and 2D NMR, HRESIMS and electronic circular dichroism experiments. All compounds were evaluated for their inhibitory effects on β-amyloid aggregation, and the optical pure compound 2b was found to show the optimal Aβ(1-42) aggregation inhibition potency (81.1% at 20 μM). In addition, despite large amount of chemical studies performed on genus Paeonia, the lignans were reported for the first time.

Topics: Amyloid beta-Peptides; Lignans; Molecular Docking Simulation; Molecular Structure; Paeonia; Peptide Fragments; Plant Roots; Protein Aggregation, Pathological

2015