Synthesis and Characterization of Acylated Polycaprolactone (PCL) Nanospheres and Investigation of Their Influence on Aggregation of Amyloid Proteins |
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| Authors: | Mojtaba Ansari Ali Akbar Moosavi Movahedi |
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| Institution: | 1. Biomaterial Group, Faculty of Biomedical Engineering, Amirkabir University of Technology, Tehran, Iran;2. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran;3. Center of Excellence in Biothermodynamics, University of Tehran, Tehran, Iran |
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| Abstract: | Acylated polycaprolactone (PCL) nanospheres were fabricated and employed to interact with amyloid-β-(25–35) peptides (Aβ25–35), "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 Aβ25–35 peptides was investigated by thioflavin T fluorescence measurements. The result showed that, without nanospheres, the Aβ25–35 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. |
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| Keywords: | acylated polycaprolactone (PCL) nanospheres Alzheimer's disease amyloid aggregation hydrophobic interaction protein misfolding thioflavin T(ThT) |
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