Bisdemethoxycurcumin, a novel potent polyphenolic compound, effectively inhibits the formation of amyloid aggregates in ALS-associated hSOD1 mutant (L38R).

Abstract excerpt

Protein misfolding is a biological process that leads to protein aggregation. Anomalous misfolding and aggregation of human superoxide dismutase (hSOD1) into amyloid aggregates is a characteristic feature of amyotrophic lateral sclerosis (ALS), a neurodegenerative illness. Thus, focusing on the L38R mutant may be a wise decision to comprehend the SOD1 disease process in ALS. We suggest that Bisdemethoxycurcumin...

Topics

• Diarylheptanoids
• Humans
• Amyotrophic Lateral Sclerosis
• Protein Aggregates
• Amyloid
• Superoxide Dismutase-1
• Mutation
• Molecular Dynamics Simulation
• Molecular Docking Simulation
• Curcumin
• Polyphenols
• Protein Aggregation, Pathological
• Hemolysis