genistein-8-c-glucoside has been researched along with Alzheimer-Disease* in 2 studies
2 other study(ies) available for genistein-8-c-glucoside and Alzheimer-Disease
| Article | Year |
|---|---|
Glucosylpolyphenols as Inhibitors of Aβ-Induced Fyn Kinase Activation and Tau Phosphorylation: Synthesis, Membrane Permeability, and Exploratory Target Assessment within the Scope of Type 2 Diabetes and Alzheimer's Disease.
Despite the rapidly increasing number of patients suffering from type 2 diabetes, Alzheimer's disease, and diabetes-induced dementia, there are no disease-modifying therapies that are able to prevent or block disease progress. In this work, we investigate the potential of nature-inspired glucosylpolyphenols against relevant targets, including islet amyloid polypeptide, glucosidases, and cholinesterases. Moreover, with the premise of Fyn kinase as a paradigm-shifting target in Alzheimer's drug discovery, we explore glucosylpolyphenols as blockers of Aβ-induced Fyn kinase activation while looking into downstream effects leading to Tau hyperphosphorylation. Several compounds inhibit Aβ-induced Fyn kinase activation and decrease pTau levels at 10 μM concentration, particularly the per- Topics: Alzheimer Disease; Amyloid beta-Peptides; Cell Membrane Permeability; Cholinesterases; Diabetes Mellitus, Type 2; Drug Discovery; Glucosides; Glycoside Hydrolases; HEK293 Cells; Humans; Induced Pluripotent Stem Cells; Molecular Structure; Phosphorylation; Polyphenols; Proto-Oncogene Proteins c-fyn; tau Proteins | 2020 |
Exploiting the therapeutic potential of 8-β-d-glucopyranosylgenistein: synthesis, antidiabetic activity, and molecular interaction with islet amyloid polypeptide and amyloid β-peptide (1-42).
8-β-d-Glucopyranosylgenistein (1), the major component of Genista tenera, was synthesized and showed an extensive therapeutical impact in the treatment of STZ-induced diabetic rats, producing normalization of fasting hyperglycemia and amelioration of excessive postprandial glucose excursions and and increasing β-cell sensitivity, insulin secretion, and circulating insulin within 7 days at a dose of 4 (mg/kg bw)/day. Suppression of islet amyloid polypeptide (IAPP) fibril formation by compound 1 was demonstrated by thioflavin T fluorescence and atomic force microscopy. Molecular recognition studies with IAPP and Aβ1-42 employing saturation transfer difference (STD) confirmed the same binding mode for both amyloid peptides as suggested by their deduced epitope. Insights into the preferred conformation in the bound state and conformers' geometry resulting from interaction with Aβ1-42 were also given by STD, trNOESY, and MM calculations. These studies strongly support 8-β-d-glucopyranosylgenistein as a promising molecular entity for intervention in amyloid events of both diabetes and the frequently associated Alzheimer's disease. Topics: Alzheimer Disease; Amyloid beta-Peptides; Animals; Benzothiazoles; Diabetes Mellitus, Experimental; Drug Design; Epitopes; Genista; Genistein; Glucosides; Humans; Hyperglycemia; Hypoglycemic Agents; Insulin; Islet Amyloid Polypeptide; Magnetic Resonance Spectroscopy; Microscopy, Atomic Force; Microscopy, Fluorescence; Oxygen; Protein Binding; Protein Conformation; Protein Kinase Inhibitors; Rats; Rats, Wistar; Streptozocin; Thiazoles | 2014 |