Phosphorylated resveratrol as a protein aggregation suppressor in vitro and in vivo

The stability of proteins in solution poses a great challenge for both technical applications and molecular biology, including neurodegenerative diseases. In this work, a phosphorylated resveratrol material was examined for its anti-aggregation properties in vitro and in vivo. Here, an anti-fibrillation effect could be measured for amyloid beta and human insulin in vitro and general anti-aggregation properties for crude chicken egg white in solution. Using a drosophila fly model for the overexpression of amyloid beta protein, changes in physiological protein aggregation and improved locomotor abilities could be observed in the presence of dietary phosphorylated resveratrol.

Automated summary

A phosphorylated resveratrol material was studied for its anti-aggregation properties, showing an anti-fibrillation effect for specific proteins in vitro and improved physiological protein aggregation and locomotor abilities in a drosophila fly model.