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Agglomeration of proteins in acoustically levitated droplets

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Abstract

An ultrasonic trap (acoustic levitator) was used as an analytical tool to allow container-free handling of proteins in small sample volumes. This trap was combined for the first time with synchrotron small-angle X-ray scattering (SAXS) for structure analysis of biological macromolecules in a solution. The microfocus beamline at BESSY was used as a source of intense X-ray radiation. Apoferritin (APO) was used as a model protein, and its aggregation behavior in a levitator was followed from a diluted solution to the solid state. Different stages of APO agglomeration were observed without solid container walls, which may influence aggregation behavior and produce a parasitic scattering background. Starting with a volume of 5 μL we analyzed the concentration dependence of APO structure factors in the range from 5 to 1,200 mg/mL (solid protein). The solution was stirred automatically due to convection inside the droplet caused by the ultrasonic field. SAXS data recording of APO was performed in time intervals of 60 s during an aggregation experiment of 30 to 60 min.

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Authors and Affiliations

  1. BAM Federal Institute for Materials Research and Testing, Richard-Willstaetter-Str. 11, 12489, Berlin, Germany

    Friedmar Delißen, Jork Leiterer, Ralf Bienert, Franziska Emmerling & Andreas F. Thünemann

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  1. Friedmar Delißen
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  2. Jork Leiterer
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  3. Ralf Bienert
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  4. Franziska Emmerling
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  5. Andreas F. Thünemann
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Correspondence to Friedmar Delißen.

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Delißen, F., Leiterer, J., Bienert, R. et al. Agglomeration of proteins in acoustically levitated droplets. Anal Bioanal Chem 392, 161–165 (2008). https://doi.org/10.1007/s00216-008-2252-0

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  • DOI: https://doi.org/10.1007/s00216-008-2252-0

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