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Single-particle optical trapping interferometry (OTI) allows us to detect theBrownian motion of a tracer bead immersed in a complex fluid with nanometricresolution and in the microsecond time-scale. By OTI, we study suspensionscomposed of filamentous actin (F-actin), a classic example of a semiflexiblepolymer, using two different kind of tracers: chemically-inert melamine resinand polystyrene depleted particles. One-particle microrheology permits toinvestigate the local fluctuations of the polymers in the network, but underthe condition of a previous knowledge of the F-actin characteristic lengths inrelation with the radius of the probes. In this work, we focus on the power-lawbehavior of the skeletal thin filament, composed by tropomyosin (Tm) andtroponin (Tn) coupled to F-actin, which has a role in the muscle contraction byits interaction with myosin. We find that the elastic modulus for theF-actin/Tm/Tn complex in the presence of Ca$^{2+}$ is constant until the limitof high frequencies, and that the calculated values of the power-law exponentare less dispersed than in F-actin alone, which we interpret as amicro-measurement of the filament stabilization.

Micro-mechanical response of the F-actin/Tropomyosin/Troponin complex by optical trapping interferometry