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Oscillations, Waves, and Interactions - GWDG

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458 S. Lakämper <strong>and</strong> C. F. Schmidt<br />

Figure 20. Effect of filament tension on the response of the active networks (actin <strong>and</strong><br />

myosin concentrations as in Fig. 19. Spectra ωC(ω)/2kBT measured with PMR at 2.5 hours<br />

(open red circles) <strong>and</strong> 9.3 hours (open blue circles) <strong>and</strong> α ′′ measured with AMR at 9.3 hours<br />

(solid blue circles) after sample preparation (initial [ATP] = 3.5 mM). In the presence of<br />

non-equilibrium activity, the response function is reduced, indicating a stiffer sample, which<br />

can be fully accounted for by prestress/tension of filaments. Theoretical predictions are<br />

shown for a network with filament tension of 0.1 pN, cross-link distance lc = 2.6 µm (green<br />

curve), <strong>and</strong> no tension with the same lc (black curve). Independently known parameters:<br />

friction coefficient z = 0.00377 Pa/s, persistence length lp = 17 × 10 −6 m, probe radius<br />

a = 2.5 mm. The system strongly violates the FD theorem <strong>and</strong> that it does so because of<br />

the contractility of the acto-myosin system [23].<br />

by biotin <strong>and</strong> neutravidin. We then measured the mechanical properties of these<br />

networks by active microrheology <strong>and</strong> found agreement with previous data from<br />

cross-linked actin networks (Fig. 19, Ref. [23]).<br />

Passive microrheology gave results that agreed completely. With ATP-energized<br />

myosin motors, however, the active processes created additional fluctuations <strong>and</strong><br />

thus violated the FD theorem [23]. The motor-generated tensions in the network also<br />

dramatically boosted the shear modulus, by up to a factor of 100 (Fig. 20).<br />

Thus, actin, myosin, <strong>and</strong> cross-links are sufficient to capture essential <strong>and</strong> general<br />

features of contractility <strong>and</strong> mechanical adaptation in cytoskeletal networks. These<br />

observations suggest mechanisms by which cells could rapidly modulate their stiffness<br />

by flexing their internal “muscles” without changing the density, polymerization, or<br />

bundling state of F-actin. Cells can actively adapt their elasticity to the mechanics<br />

of the extracellular matrix or to an externally applied force, <strong>and</strong> motors could be the<br />

cause for that. From a materials perspective, this in vitro model system exhibits an<br />

active state of matter that adjusts its own mechanical stiffness via internal forces.<br />

This work can be a starting point for exploring both model systems <strong>and</strong> cells in

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