Synthesis and Characterization of Acylated Polycaprolactone (PCL) Nanospheres and Investigation of Their Influence on Aggregation of Amyloid Proteins

Abstract

Acylated polycaprolactone (PCL) nanospheres were fabricated and employed to interact with amyloid-β-(25–35) peptides (Aβ_25–35), "peptide 11 of the 40 peptide full amyloid-β". The nanospheres were characterized by scanning electron microscopy (SEM), attenuated total reflectance Fourier transform infrared (ATR-FTIR) spectroscopy, and dynamiclightscattering (DLS), all of which confirmed that the acylated polycaprolactone (Ac-PCL) nanospheres were successfully fabricated. The effect of the nanospheres on the aggregation of Aβ_25–35 peptides was investigated by thioflavin T fluorescence measurements. The result showed that, without nanospheres, the Aβ_25–35 peptides aggregated gradually from monomers and oligomers to long fibrils with increasing incubation time. In comparison, the nanospheres were effective in interfering with fibrillogenesis and aggregation of amyloid-β. We suggest this study may contribute to the development of new therapeutic strategies against amyloid-related disorders.

Keywords:

• acylated polycaprolactone (PCL) nanospheres
• Alzheimer's disease
• amyloid aggregation
• hydrophobic interaction
• protein misfolding
• thioflavin T(ThT)