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Biomimetic models of the actin cortex

MPS-Authors
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Haraszti,  Tamas
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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Schulz,  Simon
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Uhrig,  Kai
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Roos,  Wouter
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Curtis,  Jennifer E.
Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Maier,  Timo
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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Clemen,  Anabel E.-M.
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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Citation

Haraszti, T., Schulz, S., Uhrig, K., Kurre, R., Roos, W., Schmitz, C. H. J., et al. (2009). Biomimetic models of the actin cortex. Biophysical Reviews and Letters, 4(1&2), 17-32. doi:10.1142/S1793048009001009.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-3DEE-C
Abstract
The cytoskeleton is an actively regulated complex network in the cell. One of the most researched components is actin. In our work we developed and tested two microfluidic systems both being applicable to construct quasi 2-dimensional biomimetic actin networks. The first system uses polydimethylsiloxane micropillars, the other polystyrene microparticles held by holographic optical tweezers as anchoring points. Our devices provide actin networks with mesh sizes from a few micrometers up to the order of 10 micrometers. Qualitative analysis shows similar network formation in both systems. Crosslinking was tested using filamin, α-actinin, Ca and Mg ions. The crosslinking process is characterized by a zipping like event, which is limited only by the high stretching modulus of the actin filaments.