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

被引:15
作者
Ansari, Mojtaba [1 ]
Salahshour-Kordestani, Soheila [1 ]
Habibi-Rezaei, Mehran [2 ,3 ]
Movahedi, Ali Akbar Moosavi [4 ,5 ]
机构
[1] Amirkabir Univ Technol, Fac Biomed Engn, Biomat Grp, Tehran, Iran
[2] Univ Tehran, Sch Biol, Coll Sci, Tehran, Iran
[3] Univ Tehran, Nanobiomed Ctr Excellence Nanosci & Nanotechnol, Res Ctr, Tehran, Iran
[4] Univ Tehran, Inst Biochem & Biophys, Tehran, Iran
[5] Univ Tehran, Ctr Excellence Biothermodynam, Tehran, Iran
来源
JOURNAL OF MACROMOLECULAR SCIENCE PART B-PHYSICS | 2015年 / 54卷 / 01期
关键词
acylated polycaprolactone (PCL) nanospheres; Alzheimer's disease; amyloid aggregation; hydrophobic interaction; protein misfolding; thioflavin T(ThT); NANOPARTICLES; FIBRILLATION; PEPTIDE; SURFACE; SIZE;
D O I
10.1080/00222348.2014.984578
中图分类号
O63 [高分子化学(高聚物)];
学科分类号
070305 ; 080501 ; 081704 ;
摘要
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.
引用
收藏
页码:71 / 80
页数:10
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