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

Johannes MehringerJuan Antonio NavarroDidier TouraudStephan SchneuwlyWerner Kunz
Published in: RSC chemical biology (2022)
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.
Keyphrases
  • protein protein
  • endothelial cells
  • type diabetes
  • amino acid
  • binding protein
  • spinal cord injury
  • transcription factor
  • metabolic syndrome
  • skeletal muscle