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Motor protein driven microtubule transport on gold particle nanopatterns

MPG-Autoren
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Blümmel,  Jacques
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Spatz,  Joachim P.
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany;

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Zitation

Blümmel, J., Cahu, J., Sandblad, L., Schmitz, C., Surrey, T., & Spatz, J. P. (2009). Motor protein driven microtubule transport on gold particle nanopatterns. Biophysical Reviews and Letters, 4(1&2), 153-162. doi:10.1142/S179304800900096X.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-3DF1-2
Zusammenfassung
Novel glass surfaces with quasi-hexagonally arranged gold nanoparticles to control motor protein immobilisation and motor protein dependent microtubule transport were applied. We first show that the kinesin-like motor protein Eg5 adsorbs efficiently and selectively to gold nanodots comprising a molecular motor nanopattern, while the glass surface between nanodots is passivated by a layer of polyethylene glycol in order to reduce non-specific interactions of individual motors with the substrate. We show that the motor nanopattern and density is indeed controlled by the gold nanodot density. We then use these motor protein arrays to investigate the kinetics of microtubule transport and find that the characteristics of the molecular motor nanopattern influence the characteristics of microtubule transport. This finding describes new biomimetic surfaces of molecularly controlled motor protein surface densities.