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

Muthuraj, Balakrishnan, Chowdhury, Sayan Roy, Iyer, Parameswar K.
ACS Applied Materials & Interfaces 2015 v.7 no.38 pp. 21226-21234
Alzheimer disease, amyloid, bioactive properties, histidine, hydrogen bonding, peptides, spectroscopy
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 results give rise to a new and unique complementary approach for modulating the biological effects of the aggregates in amyloidogenic peptides.