Nanoscale Size Control of Protein Aggregates

Authors

  • Christian Pedersen,

    Corresponding author
    1. Department of Engineering Sciences, Nanotechnology and Functional Materials, The Ångström Laboratory, Uppsala University, 751 21 Uppsala, Sweden
    Current affiliation:
    1. Department of Pharmacy, The Uppsala Biomedical Centre, Uppsala University, Box 580, 751 23 Uppsala, Sweden
    • Department of Engineering Sciences, Nanotechnology and Functional Materials, The Ångström Laboratory, Uppsala University, 751 21 Uppsala, Sweden.
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  • Helen Vallhov,

    1. Department of Medicine Solna, Translational Immunology Unit, Karolinska Institutet and Karolinska University Hospital, 171 76 Stockholm, Sweden
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  • Håkan Engqvist,

    1. Department of Engineering Sciences, Applied Materials Science, The Ångström Laboratory, Uppsala University, 751 21 Uppsala, Sweden
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  • Annika Scheynius,

    1. Department of Medicine Solna, Translational Immunology Unit, Karolinska Institutet and Karolinska University Hospital, 171 76 Stockholm, Sweden
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  • Maria Strømme

    Corresponding author
    1. Department of Engineering Sciences, Nanotechnology and Functional Materials, The Ångström Laboratory, Uppsala University, 751 21 Uppsala, Sweden
    • Department of Engineering Sciences, Nanotechnology and Functional Materials, The Ångström Laboratory, Uppsala University, 751 21 Uppsala, Sweden.
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Abstract

Herein, a novel method to synthesize soluble, sub-micrometer sized protein aggregates is demonstrated by mixing native and denatured proteins without using bacteria and contaminating proteins. Ovalbumin (OVA) is employed as a model protein. The average size of the formed aggregates can be controlled by adjusting the fraction of denatured protein in the sample and it is possible to make unimodal size distributions of protein aggregates. OVA aggregates with a size of ∼95 nm are found to be more immunogenic compared to native OVA in a murine splenocyte proliferation assay. These results suggest that the novel method of engineering size specific sub-micrometer sized aggregates may constitute a potential route to increasing the efficacy of protein vaccines. The protein aggregates may also be promising for use in other applications including the surface functionalization of biomaterials and as industrial catalysis materials.

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