TY - JOUR
T1 - Synthesis and characterization of fluorinated magnetic core-shell nanoparticles for inhibition of insulinamyloid fibril formation
AU - Skaat, Hadas
AU - Belfort, Georges
AU - Margel, Shlomo
PY - 2009
Y1 - 2009
N2 - Maghemite (γ-Fe2O3) magnetic nanoparticles of 15.0 2.1nm are formed by nucleation followed by controlled growth of maghemite thin films on gelatin-iron oxide nuclei. Uniform magnetic γ-Fe 2O3/poly (2,2,3,3,4,4,4-heptafluorobutyl acrylate) (γ-Fe2O3/PHFBA) core-shell nanoparticles are prepared by emulsion polymerization of the fluorinated monomer 2,2,3,3,4,4,4-heptafluorobutyl acrylate (HFBA) in the presence of the maghemite nanoparticles. The kinetics of the insulin fibrillation process in the absence and in the presence of the γ-Fe2O3/PHFBA core-shell nanoparticles are elucidated. A significant direct slow transition from α-helix to β-sheets during insulin fibril formation is observed in the presence of the γ-Fe2O3/PHFBA nanoparticles. This is in contradiction to our previous manuscript, which illustrated that the γ-Fe2O3 core nanoparticles do not affect the kinetics of the formation of the insulin fibrils, and to other previous publications that describe acceleration of the fibrillation process by using various types of nanoparticles. These core-shell nanoparticles may therefore be also useful for the inhibition of conformational changes of other amyloidogenic proteins that lead to neurodegenerative diseases such as Alzheimer's, Parkinson's, Huntington's, mad cow and prion diseases.
AB - Maghemite (γ-Fe2O3) magnetic nanoparticles of 15.0 2.1nm are formed by nucleation followed by controlled growth of maghemite thin films on gelatin-iron oxide nuclei. Uniform magnetic γ-Fe 2O3/poly (2,2,3,3,4,4,4-heptafluorobutyl acrylate) (γ-Fe2O3/PHFBA) core-shell nanoparticles are prepared by emulsion polymerization of the fluorinated monomer 2,2,3,3,4,4,4-heptafluorobutyl acrylate (HFBA) in the presence of the maghemite nanoparticles. The kinetics of the insulin fibrillation process in the absence and in the presence of the γ-Fe2O3/PHFBA core-shell nanoparticles are elucidated. A significant direct slow transition from α-helix to β-sheets during insulin fibril formation is observed in the presence of the γ-Fe2O3/PHFBA nanoparticles. This is in contradiction to our previous manuscript, which illustrated that the γ-Fe2O3 core nanoparticles do not affect the kinetics of the formation of the insulin fibrils, and to other previous publications that describe acceleration of the fibrillation process by using various types of nanoparticles. These core-shell nanoparticles may therefore be also useful for the inhibition of conformational changes of other amyloidogenic proteins that lead to neurodegenerative diseases such as Alzheimer's, Parkinson's, Huntington's, mad cow and prion diseases.
UR - http://www.scopus.com/inward/record.url?scp=67649148203&partnerID=8YFLogxK
U2 - 10.1088/0957-4484/20/22/225106
DO - 10.1088/0957-4484/20/22/225106
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C2 - 19433878
AN - SCOPUS:67649148203
SN - 0957-4484
VL - 20
JO - Nanotechnology
JF - Nanotechnology
IS - 22
M1 - 225106
ER -