Movement of fluorescently labeled microtubules over a kinesin-coated glass surface in the presence of ATP (gliding motility assay). All microtubules move with similar speed (about 800nm/s) but their direction is completely arbitrary.

Directed movement of gliding microtubules along topographically structured microchannels on the surface of a coverslip. The channels are a replica mold of a silicon master (channel width 500nm, periodicity 1000nm, depth 300nm) produced using a PDMS stamp as an intermediate [1].

Kinesin-driven, unidirectional movement of rhodamine-labeled microtubules (red) along a chemically and topographically structured silicon chip. The bottom of the channels (green – depth 300 nm), is coated with kinesin. The surrounding regions are blocked by polyethylene glycol [1, 2].In this geometry the electrical docking of microtubules to given surface areas could be demonstarted [3].

Collaboration with the group of C. Dekker (Delft University of Technology, The Netherlands).

Biotemplated nanopatterning of planar surfaces with molecular motors (I): Kinesin-1 molecules, which are bound to the lattice of a 'template' microtubule are transferred onto the surface by a stamping process. The stamped kinesin-1 motors (green) then move and guide the 'transport' microtubules (red) [4].

Biotemplated nanopatterning of planar surfaces with molecular motors (II): Kinesin-14 (Ncd) molecules, are bound via their second binding site to surface-immobilized 'template' microtubules (dim). 'Transport' microtubules (bright) then follow the motor tracks on the template microtubules [4].

Using a computer-programmable micro perfusion system (MicCell™ - developed in collaboration with GeSiM mbH, Grosserkmannsdorf, Germany) gliding microtubules were redirected by hydrodynamic flow (0.5 ul/s) [5].

Start and stop of microtubule motility upon fast exchanging motility solutions with ATP or AMPPNP (a non-hydrolyzable analogue of ATP) in the MicCell™ system [5].

Control of microtubule motility on switchable polymer surfaces. Kinesin motors are embedded between thermoresponsive PNIPAM molecules on a substrate surface. Repeated changes in the temperature result in the reversible switching of PNIPAM chains between the expanded conformation (where microtubules are repelled from the surface) and the collapsed conformation (where microtubules can glide unhindered on the kinesin molecules) [6].

Collaboration with the group of M. Stamm (Leibniz Institute for Polymer Research Dresden).