Student project 1 (Laura Heinen)

Project 1: Membrane enzymology meets materials world 

Membrane proteins function as the gates of molecular transport in the cell. They are crucial players e.g. to sustain homeostasis or for the active uptake of substrates, i.e. the molecular transport across a membrane against an unfavorable energy potential. To study and make use of membrane proteins outside their natural environment, they are classically reconstituted into biomimetic lipid vesicles.(1) Such proteoliposomes are optimized to retain the enzyme activity, but often suffer from intrinsically low structural stability. Hence, this hampers the use of membrane proteins over prolonged timescales and in a materials context.

In this project, we aim to connect membrane proteins with synthetic materials to build functional non-equilibrium systems. To this end, we target more robust and stable synthetic vesicle systems based on block-copolymers, DNA amphiphiles, lipids and hybrid compositions thereof. The challenge is to keep the membrane proteins fully functional in these more rigid systems without severe loss of activity.

You will be first involved in the design of synthetic vesicles and then in the biochemical characterization of the reconstituted membrane proteins. The reconstituted synthetic systems will be benchmarked against classical proteoliposome protocols in our group. Thus, within this project you will likewise get deeper insight into the biochemistry, characterization and handling of membrane proteins as well as basic polymer chemistry and the physicochemical self-assembly of vesicular structures. The focus of this project is on experimental work including the analysis of kinetic enzyme assays, various microscopy and light scattering techniques.

(1) E. R. Geertsma et al., Nat. Protoc., 2008, 3, 256–266