Preparation of amyloid-like fibrils containing magnetic iron oxide nanoparticles: Effect of protein aggregation on proton relaxivity
- Biomolecular and Organic Electronics, Department of Physics, Chemistry, and Biology (IFM), Linkoeping University, SE-581 83 Linkoeping (Sweden)
- Molecular Surface Physics and Nano Science, Department of Physics, Chemistry, and Biology (IFM), Linkoeping University, SE-581 83 Linkoeping (Sweden)
Highlights: Black-Right-Pointing-Pointer Preparation of amyloid materials labeled with magnetic iron oxide nanoparticles. Black-Right-Pointing-Pointer Characterization of amyloid materials by electron tomography. Black-Right-Pointing-Pointer 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.
- OSTI ID:
- 22207767
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 419, Issue 4; Other Information: Copyright (c) 2012 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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