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Allium roseum L. extract inhibits amyloid beta aggregation and toxicity involved in Alzheimer's disease.
Boubakri, Abdelbasset; Leri, Manuela; Bucciantini, Monica; Najjaa, Hanen; Ben Arfa, Abdelkarim; Stefani, Massimo; Neffati, Mohamed.
Affiliation
  • Boubakri A; Laboratoire des Ecosystèmes Pastoraux et Valorisation des Plantes Spontanées et des Micro-organismes Associés, Institut des Régions Arides, Médenine, Tunisia.
  • Leri M; Department of Biology, Faculty of Sciences, University of Gabes, Cité Erriadh, Zrig Gabès, Tunisia.
  • Bucciantini M; Department of Clinical and Experimental Biomedical Sciences "Mario Serio", University of Florence, Viale Morgagni, Florence, Italy.
  • Najjaa H; Department of Neuroscience, Psychology, Area of Medicine and Health of the Child, University of Florence, Viale Pieraccini, Florence, Italy.
  • Ben Arfa A; Department of Clinical and Experimental Biomedical Sciences "Mario Serio", University of Florence, Viale Morgagni, Florence, Italy.
  • Stefani M; Laboratoire des Ecosystèmes Pastoraux et Valorisation des Plantes Spontanées et des Micro-organismes Associés, Institut des Régions Arides, Médenine, Tunisia.
  • Neffati M; Laboratoire des Ecosystèmes Pastoraux et Valorisation des Plantes Spontanées et des Micro-organismes Associés, Institut des Régions Arides, Médenine, Tunisia.
PLoS One ; 15(9): e0223815, 2020.
Article in En | MEDLINE | ID: mdl-32997672
Allium roseum is an important medicinal and aromatic plant, specific to the North African flora and a rich source of important nutrients and bioactive molecules including flavonoids and organosulfur compounds whose biological activities and pharmacological properties are well known. In the present study, the inhibition of amyloid beta protein toxicity by the ethanolic extract of this plant is investigated for the first time. Preliminary biochemical analyses identified kæmpferol and luteolin-7-o-glucoside as the more abundant phenolic compounds. The effects of A. roseum extract (ARE) on aggregation and aggregate cytotoxicity of amyloid beta-42 (Aß42), whose brain aggregates are a hallmark of Alzheimer's disease, were investigated by biophysical (ThT assay, Dynamic light scattering and transmission electron microscopy) and cellular assays (cytotoxicity, aggregate immunolocalization, ROS measurement and intracellular Ca2+ imaging). The biophysical data suggest that ARE affects the structure of the Aß42 peptide, inhibits its polymerization, and interferes with the path of fibrillogenesis. The data with cultured cells shows that ARE reduces Aß42 aggregate toxicity by inhibiting aggregate binding to the cell membrane and by decreasing both oxidative stress and intracellular Ca2+. Accordingly, ARE could act as a neuroprotective factor against Aß aggregate toxicity in Alzheimer's disease.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Peptide Fragments / Allium / Plant Extracts / Amyloid beta-Peptides / Neuroprotective Agents / Alzheimer Disease / Protein Aggregation, Pathological Type of study: Prognostic_studies Limits: Humans Language: En Journal: PLoS One Journal subject: CIENCIA / MEDICINA Year: 2020 Document type: Article Affiliation country: Tunisia Country of publication: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Peptide Fragments / Allium / Plant Extracts / Amyloid beta-Peptides / Neuroprotective Agents / Alzheimer Disease / Protein Aggregation, Pathological Type of study: Prognostic_studies Limits: Humans Language: En Journal: PLoS One Journal subject: CIENCIA / MEDICINA Year: 2020 Document type: Article Affiliation country: Tunisia Country of publication: United States