The study of protein motion inside microemulsions has relevance with respect to applications since microemulsions are interesting reaction media for enzyme catalyzed reactions with oil soluble substrates. Moreover, due to their variable composition microemulsions allow to tune the dimensions of the oil and water domains. In this contribution, we use this possibility to generate variable soft confinement of proteins in sugar surfactant and oligoethyleneglycol alkyether based bicontinuous microemulsions. As a model protein we employ GFP. The structure of the microemulsion matrix is studied by small angle scattering techniques. The protein motion inside the microemulsion is followed by fluorescence correlation spectroscopy (FCS). We observe a transition to sub-diffusional motion upon decreasing the water domain size. In addition to the FCS experiments, also the use of neutron spin-echo spectroscopy (NSE) to follow enzyme motion in complex fluid media will be discussed and first preliminary experiments will be shown.

Protein diffusion in a bicontinuous microemulsion: sub-diffusion by tunable soft confinement

254th National Meeting (2017)

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