Austria : PhD student positions: Downstream Processing at BOKU Vienna

The International PhD Programme Biomolecular Technology of Proteins (http://biotop.boku.ac.at) two research projects are offered by the Working Group Downstream Processing  (Area 4, Supervisor: Alois Jungbauer):

Project 1: Binding tropism of large biomolecules on grafted and non-grafted porous chromatography media

Large proteins, plasmids and viruses are interesting and potential candidates for biopharmaceuticals, but their adsorption behaviour on chromatography media is poorly understood. Usually ion-exchange chromatography is the workhorse for their separation and requires porous media with large pores. Polymer-grafted ion exchangers have been shown to exhibit a significantly higher adsorption capacity compared to non-grafted media. In this project the adsorption mechanism of theses large biomolecules should be investigated on a molecular level and linked to thermodynamical analysis to understand the driving forces for the adsorption.  Binding at molecular and surface level should be assed by NMR, SAXS, CryoSEM and conventional adsorption studies. Thermodynamical analysis will be made by titration calorimetry, and retention analysis at different temperature interpreted by vant’ Hoff analysis.  A model should be derived to predict the analysis of these large biomolecules.

Project 2: Influence of surface curvature on unfolding of proteins on nanoparticles

Protein adsorption plays a crucial role in various fields in biotechnology and biomedical engineering. Nanoparticles could be an interesting alternative to conventional chromatography media. In case of nanoparticles, it is not clear how proteins adsorb on their surface. Nanoparticles have only a micropore-structure which does not contribute to the surface available for binding of proteins. However it is not clear how the curvature of the particle affects the adsorbing protein. So we want to distinguish between the effects on protein deformation caused by the curvature and the effects caused by the surface energy. The extent of partial unfolding will be assessed by attenuated total reflection Fourier transform infrared (ATR-FT-IR) spectroscopy that monitors changes in the secondary structure. A method to measure the surface energy will be developed using a similar approach as previously described with inverse gas chromatography. Furthermore, unfolding will be studied with different adiabatic compressibility. To bridge the gap to bioseparation, desorption experiments must be conducted to see how efficiently the protein can be removed from such nanoparticles.

Application:

For detailed information on research projects, application guidelines and download of forms please visit: http://biotop.boku.ac.at

Application deadline: September 30th, 2010

Further Information

Application Deadline : 30 September 2010

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Contact Adress: http://biotop.boku.ac.at

Contact Email: biotop@boku.ac.at

Posted on 2010-08-12 03:54:17

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