By consuming energy from the hydrolysis of ATP, cells are able to exert forces that stem from biochemical reactions. A central element of cells is the cytoskeleton, which is mainly composed of microtubules and actin filaments and accounts for the architecture and most of the mechanical properties of the cells. It is made of crosslinked polymers and, in terms of rheology, has a viscoelastic behavior. Within the cytoskeleton, processes such as actin or microtubule polymerization can exert forces. Proteins from the molecular motor family have the specific role of converting the energy stored in chemical form into mechanical energy. The out-of-equilibrium mechanical activity of the cell is directly related to these forces of biochemical origin. In this work, we studied the statistical distribution of biochemical forces exerted on a micrometer-sized bead attached to the actin cortex through cell adhesion receptors: integrins. The study of the forces of biological origin is inseparable from knowledge of the forces of thermal origin because, at this microscopic scale, the contribution of thermal forces is not negligible. The forces acting on the probe have two possible origins: biological or thermal. Our experimental approach is based on the combination of two microrheology techniques, active and passive, which allows us to calculate the temporal autocorrelation function of the forces exerted on a probe attached to the cortical actin and compare it to the autocorrelation function of the estimated thermal forces via the fluctuation-dissipation theorem. The difference between these two spectra gives us an idea of the contribution of the forces of biological origin to the movement of the bead and a measure of the deviation of the system from thermodynamic equilibrium. To further investigate this system, i.e. a bead undergoing forces from the cortical actin, we studied the effect of varying the ligand coating density on the bead. The question that has driven us throughout this work is the origin of these biological forces or, more precisely the nature of the component of the cytoskeleton that exerts these athermal forces. Initially, we studied the influence of temperature on these biological forces. We then studied the effect of depletion of ATP in the cell, of the depolymerization of actin and of the inhibition of molecular motors of the myosin family.
