Inhibition of Amyloid-like Fibril Formation of Trypsin by Red Wines

Protein Pept Lett. 2017;24(5):466-470. doi: 10.2174/0929866524666170214125847.

Abstract

The aim of the present study was to examine the potential role and applicability of dietary supplements in reducing the risk of development of amyloid diseases associated with the gastrointestinal tract, such as type II diabetes. Trypsin, a well-known serine protease was used as a model protein in our experiments. The effect of various red wines on the formation of amyloid-like fibrils of trypsin was studied in vitro, in aqueous ethanol, at pH 7.0. Turbidity measurements, aggregation kinetics experiments, Congo red binding assays and electronic circular dichroism spectroscopic measurements were used to follow the aggregation process in the presence or absence of various red wines. The results suggest that red wines effectively inhibit the formation of amyloid-like fibrils of trypsin and the inhibitory effect is dose-dependent. The extent of inhibition was found to be proportional to the total concentration of phenolic compounds.

Keywords: Amyloid-like fibrils; congo red; electronic circular dichroism; natural polyphenols; red wine; trypsin.

MeSH terms

  • Amyloid* / chemistry
  • Amyloid* / drug effects
  • Amyloid* / metabolism
  • Animals
  • Cattle
  • Circular Dichroism
  • Congo Red
  • Kinetics
  • Phenols / pharmacology
  • Trypsin* / chemistry
  • Trypsin* / drug effects
  • Trypsin* / metabolism
  • Wine*

Substances

  • Amyloid
  • Phenols
  • Congo Red
  • Trypsin