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

Acylated polycaprolactone (PCL) nanospheres were fabricated and employed to interact with amyloid-beta-(25-35) peptides (A beta(25-35)), "peptide 11 of the 40 peptide full amyloid-beta". 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 A beta(25-35) peptides was investigated by thioflavin T fluorescence measurements. The result showed that, without nanospheres, the A beta(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-beta. We suggest this study may contribute to the development of new therapeutic strategies against amyloid-related disorders.