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

J Med Chem. 2020 Oct 22;63(20):11663-11690. doi: 10.1021/acs.jmedchem.0c00841. Epub 2020 Oct 13.

Abstract

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-O-methylated glucosylacetophloroglucinol and the 4-glucosylcatechol dibenzoate, the latter inhibiting also butyrylcholinesterase and β-glucosidase. Both compounds are nontoxic with ideal pharmacokinetic properties for further development. This work ultimately highlights the multitarget nature, fine structural tuning capacity, and valuable therapeutic significance of glucosylpolyphenols in the context of these metabolic and neurodegenerative disorders.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alzheimer Disease / drug therapy*
  • Alzheimer Disease / metabolism
  • Amyloid beta-Peptides / metabolism*
  • Cell Membrane Permeability / drug effects
  • Cholinesterases / metabolism
  • Diabetes Mellitus, Type 2 / drug therapy*
  • Diabetes Mellitus, Type 2 / metabolism
  • Drug Discovery / methods
  • Glucosides / chemical synthesis*
  • Glucosides / chemistry
  • Glucosides / pharmacology
  • Glycoside Hydrolases / antagonists & inhibitors
  • HEK293 Cells
  • Humans
  • Induced Pluripotent Stem Cells / drug effects
  • Induced Pluripotent Stem Cells / metabolism
  • Molecular Structure
  • Phosphorylation
  • Polyphenols / chemical synthesis*
  • Polyphenols / chemistry
  • Polyphenols / pharmacology
  • Proto-Oncogene Proteins c-fyn / antagonists & inhibitors*
  • tau Proteins / metabolism*

Substances

  • Amyloid beta-Peptides
  • Glucosides
  • Polyphenols
  • tau Proteins
  • Proto-Oncogene Proteins c-fyn
  • Cholinesterases
  • Glycoside Hydrolases