Phosphorylated resveratrol as a protein aggregation suppressor in vitro and in vivo. Issue 2 (11th January 2022)

• Record Type: Journal Article
• Authors: Mehringer, Johannes; Navarro, Juan Antonio; Touraud, Didier; Schneuwly, Stephan; Kunz, Werner
• Is Part Of: RSC chemical biology. Volume 3:Issue 2(2022)
• Page Start: 250
• Page End: 260
• Publication Date: 2022-01-11
• Subjects: 572
• DOI: 10.1039/d1cb00220a
• Languages: English
• ISSNs: 2633-0679

Abstract

Abstract : Phosphorylated resveratrol can prevent the aggregation of globular and intrinsically disordered proteins in vitro and in vivo . Abstract : 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.