Modulation of Amyloid-β Fibrils into Mature Microrod-Shaped Structure by Histidine Functionalized Water-Soluble Perylene Diimide

Alzheimer’s disease (AD) is associated with different types of amyloid peptide aggregates including senile plaques, fibrils, protofibrils, and oligomers. Due to these difficulties, a powerful strategy is needed for the disaggregation of amyloid aggregates by modulating their self-aggregation behavior. Herein, we report a unique approach toward transforming the aggregated amyloidogenic peptides using an amino acid functionalized perylene diimide as a molecular modulator, which is a different nondestructive approach as compared to inhibiting the aggregation of peptides. The histidine functionalized perylenediimide (PDI–HIS) molecule could coassemble with amyloid β (Aβ) peptides via hydrogen bonding that leads to the enhancement in the π–π interactions between Aβ and PDI–HIS moieties. The Thioflavin T (ThT) assay and various spectroscopic and microscopic techniques establish that the PDI–HIS molecules accelerate the Aβ1–40 and the amyloid aggregates in CSF into micro size coassembled structures. These result...