α-Synuclein binding activity of the plant growth promoter asterubine

Preventing the aggregation of certain amyloid proteins has the potential to slow down the progression of diseases like Alzheimer's, Parkinson's, and type 2 diabetes mellitus. During a high-throughput screen of 300 Australian marine invertebrate extracts, the extract of the marine sponge Thorectandra sp. 4408 displayed binding activity to the Parkinson's disease-associated protein, alpha-synuclein. Isolation of the active component led to its identification as the known plant growth promoter asterubine (1). This molecule shares distinct structural similarities with potent amyloid beta aggregation inhibitors tramiprosate (homotaurine) and ALZ-801. Herein we report the isolation, NMR data acquired in DMSO and alpha-synuclein binding activity of asterubine (1).

Automated summary

This article introduces the potential of preventing the aggregation of certain amyloid proteins to slow down the progression of diseases like Alzheimer's, Parkinson's, and type 2 diabetes mellitus. Through a high-throughput screen of 300 Australian marine invertebrate extracts, the extract of the marine sponge Thorectandra sp. 4408 showed binding activity to the Parkinson's disease-associated protein, alpha-synuclein. The active component isolated from this extract was identified as the known plant growth promoter asterubine (1), which shares structural similarities with amyloid beta aggregation inhibitors tramiprosate (homotaurine) and ALZ-801. This study reports the isolation, NMR data acquired in DMSO, and alpha-synuclein binding activity of asterubine (1).