Published March 23, 2012 | Version v1
Journal article

Preparation of amyloid-like fibrils containing magnetic iron oxide nanoparticles: Effect of protein aggregation on proton relaxivity

  • 1. Biomolecular and Organic Electronics, Department of Physics, Chemistry, and Biology (IFM), Linköping University, SE-581 83 Linköping (Sweden)
  • 2. Molecular Surface Physics and Nano Science, Department of Physics, Chemistry, and Biology (IFM), Linköping University, SE-581 83 Linköping (Sweden)

Description

Highlights: ► Preparation of amyloid materials labeled with magnetic iron oxide nanoparticles. ► Characterization of amyloid materials by electron tomography. ► Influence of protein aggregation on the magnetic nanoparticle properties. -- Abstract: A method to prepare amyloid-like fibrils functionalized with magnetic nanoparticles has been developed. The amyloid-like fibrils are prepared in a two step procedure, where insulin and magnetic nanoparticles are mixed simply by grinding in the solid state, resulting in a water soluble hybrid material. When the hybrid material is heated in aqueous acid, the insulin/nanoparticle hybrid material self assembles to form amyloid-like fibrils incorporating the magnetic nanoparticles. This results in magnetically labeled amyloid-like fibrils which has been characterized by Transmission Electron Microscopy (TEM) and electron tomography. The influence of the aggregation process on proton relaxivity is investigated. The prepared materials have potential uses in a range of bio-imaging applications.

Availability note (English)

Available from http://dx.doi.org/10.1016/j.bbrc.2012.02.077

Additional details

Identifiers

DOI
10.1016/j.bbrc.2012.02.077;
PII
S0006-291X(12)00310-5;

Publishing Information

Journal Title
Biochemical and Biophysical Research Communications
Journal Volume
419
Journal Issue
4
Journal Page Range
p. 682-686
ISSN
0006-291X
CODEN
BBRCA9

Optional Information

Copyright
Copyright (c) 2012 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.