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-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 tr...

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Bibliographic Details
Published in:Journal of macromolecular science. Physics 2015-01, Vol.54 (1), p.71-80
Main Authors: Ansari, Mojtaba, Salahshour-Kordestani, Soheila, Habibi-Rezaei, Mehran, Movahedi, Ali Akbar Moosavi
Format: Article
Language:English
Subjects:
acylated polycaprolactone (PCL) nanospheres
Agglomeration
Alzheimer's disease
amyloid aggregation
Fluorescence
hydrophobic interaction
Monomers
Nanospheres
Oligomers
Peptides
Polycaprolactone
protein misfolding
Scanning electron microscopy
thioflavin T(ThT)
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Summary: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.
ISSN:0022-2348
1525-609X
DOI:10.1080/00222348.2014.984578