Agglomeration of proteins in acoustically levitated droplets |
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Authors: | Friedmar Delißen Jork Leiterer Ralf Bienert Franziska Emmerling Andreas F Thünemann |
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Institution: | BAM Federal Institute for Materials Research and Testing, Richard-Willstaetter-Str. 11, 12489, Berlin, Germany. friedmar.delissen@bam.de |
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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 microL 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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