Effect of maghemite nanoparticles on insulin amyloid fibril formation: Selective labeling, kinetics, and fibril removal by a magnetic field

Hadas Skaat, Mirco Sorci, Georges Belfort, Shlomo Margel

Research output: Contribution to journalArticlepeer-review

58 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)342-351
Number of pages10
JournalJournal of Biomedical Materials Research - Part A
Volume91
Issue number2
DOIs
StatePublished - Nov 2009

Keywords

  • Insulin amyloid fibrils
  • Magnetic nanoparticles
  • Neurodegenerative diseases
  • Protein folding
  • γ-FeO nanoparticles

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