2017
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2014
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My research focus is on the effect of vesicles on enzyme-catalyzed radical polymerizations. Vesicles are assemblies of amphiphiles which form a self-closed bilayer, entrapping part of the aqueous solution in which they are suspended. In my case, the vesicles are formed by the surfactant sodium bis(2-ethylhexyl) sulfosuccinate (AOT). They have a diameter of approximately 80 nm and a bilayer thickness of 2 nm.
We have found that the vesicles act as templates and guide enzymatic polymerizations towards desired polymeric end-products, which form a stable colloid with the vesicles. This is in contrast to the enzymatic polymerization in the absence of vesicles, where the products are found to be chemically different and precipitate. This has been seen for a number of oxidative enzymes and monomers: soybean peroxidase, horseradish peroxidase and Trametes versicolor laccase (TvL), and aniline, pyrrol and p-aminodiphenylamine.
At the moment I am working on elucidating the molecular mechanism behind the observed template-effect of the vesicles. Strategies include HPLC-UV-Vis, HPLC-MS in combination with labelling experiments, such as selective deuteration of the monomer in order to elucidate the structure of the oligomers.