Amyloid fibrils, including β-amyloid (Aβ) fibrils, are protein aggregates that form under certain conditions, associated with neurodegeneration that interfere with neural synaptic transmission resulting in some neural disorders, such as Alzheimer's disease. The aim of this study is to inhibit amyloidogenesis by using preparatory polymeric nanomicelles as therapeutic agents and also as nanocarriers for curcumin to target Aβ fibrils through the glycation method of bovine serum albumin (BSA) in the presence of phosphate-buffered saline. Polymeric nanomicelles were prepared from phosphatidylethanolamine-distearoyl methoxypolyethylene glycol conjugates in the presence and absence of curcumin and then the morphological and structural characteristics of the nanomicelles were characterized in detail. Following the preparation of unloaded and curcumin-loaded nanomicelles with the desired size and properties, their effects on BSA glycation/fibrillation process were investigated. The samples were analyzed by thioflavin T (ThT) fluorescence and advanced glycation end (AGE) products autofluorescence measurements. The results showed that ThT fluorescence related to the formation of β-sheets and AGE autofluorescence (associated with AGE production) decreased in the presence of curcumin-loaded nanomicelles more than other samples. In conclusion, the promising effect of curcumin-loaded nanomicelles on inhibition of amyloidogenesis through glycation process due to curcumin release and thus their ability to prevent the formation and accumulation of amyloid fibrils and so to suppress the Alzheimer's disease progression has been proven and can go for further investigations.
Keywords: Alzheimer's disease; amyloid fibrils; amyloidogenesis; curcumin; glycation; β-sheets.
© 2019 International Union of Biochemistry and Molecular Biology, Inc.