Self‐assembled Protein Fibril‐metal Oxide Nanocomposites

Protein aggregation is commonly associated with the onset and development of neurodegenerative disorders, including Alzheimer's, Parkinson's and other forms of pathological disorders. While this phenomenon has historically been studied in the context of its relevance to human health, over...

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Bibliographic Details
Published in:Israel journal of chemistry 2017-07, Vol.57 (7-8), p.724-728
Main Authors: Levin, A., Mason, T. O., Knowles, T. P. J., Shimanovich, U.
Format: Article
Language:English
Subjects:
Agglomeration
Assemblies
Biomedical materials
Disorders
Iron oxides
Lysozyme
Microfluidic
Microfluidics
Nanocomposites
Nanomaterials
Organic-non-organic
Protein
Proteins
Self-assembly
Surgical implants
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Summary:Protein aggregation is commonly associated with the onset and development of neurodegenerative disorders, including Alzheimer's, Parkinson's and other forms of pathological disorders. While this phenomenon has historically been studied in the context of its relevance to human health, over the past decade significant research effort has focused on utilizing amyloid‐like protein assemblies as building blocks for the development of functional biomaterials and a number of protein‐based functional materials have been demonstrated. Here we extend this concept by synthesizing hybrid organic/inorganic microcapsules containing metal‐based NPs and protein nanofibrils as a nanocomposite. To this effect, we exploit the propensity of lysozyme to self‐assemble into amyloid nanofibrils and their functionalization by carboxyl‐modified Fe3O4 NPs. We use a microfluidics‐based approach to control the micron scale moprhology of the newly formed nanocomposites. Our results illustrate the potential ofthis strategy as a platform for fabricating microcapsules from nanofibril‐inorganic NPs hybrid materials.
ISSN:0021-2148
1869-5868
DOI:10.1002/ijch.201600118