TY - JOUR
T1 - Effect of maghemite nanoparticles on insulin amyloid fibril formation
T2 - Selective labeling, kinetics, and fibril removal by a magnetic field
AU - Skaat, Hadas
AU - Sorci, Mirco
AU - Belfort, Georges
AU - Margel, Shlomo
PY - 2009/11
Y1 - 2009/11
N2 - Maghemite (γ-Fe2O3) magnetic nanoparticles of 15.0 ± 2.1 nm were formed by nucleation followed by controlled growth of maghemite thin films on gelatin-iron oxide nuclei. Human insulin amyloid fibrils were formed by incubating the monomeric insulin dissolved in aqueous continuous phase at pH 1.6 and 65°C. Magnetic human insulin amyloid fibrils/γ-Fe2O3 nanoparticle assemblies were prepared by interacting the γ-Fe2O3 nanoparticles with the insulin amyloid fibrils during or after their formation. The nanoparticles attached selectively to the insulin fibrils in both cases. The kinetics of the insulin fibrillation process in the absence and the presence of the γ-Fe2O3 nanoparticles was elucidated. The insulin amyloid fibrils/γ-Fe2O3 nanoparticle assemblies were easily extracted from the aqueous phase via a magnetic field. We hypothesize that this selective extraction approach may also be applicable for the removal of other amyloidogenic proteins that lead to neurodegenerative diseases (e.g., Alzheimer's, Parkinson's, Huntington's, mad cow, and prion diseases) from their continuous phase, e.g. milk, blood, neurological fluid, etc.
AB - Maghemite (γ-Fe2O3) magnetic nanoparticles of 15.0 ± 2.1 nm were formed by nucleation followed by controlled growth of maghemite thin films on gelatin-iron oxide nuclei. Human insulin amyloid fibrils were formed by incubating the monomeric insulin dissolved in aqueous continuous phase at pH 1.6 and 65°C. Magnetic human insulin amyloid fibrils/γ-Fe2O3 nanoparticle assemblies were prepared by interacting the γ-Fe2O3 nanoparticles with the insulin amyloid fibrils during or after their formation. The nanoparticles attached selectively to the insulin fibrils in both cases. The kinetics of the insulin fibrillation process in the absence and the presence of the γ-Fe2O3 nanoparticles was elucidated. The insulin amyloid fibrils/γ-Fe2O3 nanoparticle assemblies were easily extracted from the aqueous phase via a magnetic field. We hypothesize that this selective extraction approach may also be applicable for the removal of other amyloidogenic proteins that lead to neurodegenerative diseases (e.g., Alzheimer's, Parkinson's, Huntington's, mad cow, and prion diseases) from their continuous phase, e.g. milk, blood, neurological fluid, etc.
KW - Insulin amyloid fibrils
KW - Magnetic nanoparticles
KW - Neurodegenerative diseases
KW - Protein folding
KW - γ-FeO nanoparticles
UR - http://www.scopus.com/inward/record.url?scp=70349466557&partnerID=8YFLogxK
U2 - 10.1002/jbm.a.32232
DO - 10.1002/jbm.a.32232
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C2 - 18980178
AN - SCOPUS:70349466557
SN - 1549-3296
VL - 91
SP - 342
EP - 351
JO - Journal of Biomedical Materials Research - Part A
JF - Journal of Biomedical Materials Research - Part A
IS - 2
ER -