Swimming microorganisms can influence the diffusion of passive particles. The effect of this swimmer-particle interaction depends on different properties, such as the hydrodynamic field of the swimmer and the relative sizes of microorganisms and particles. We investigated an enhancement of the diffusion of silica doublets in a suspension of microalgae Chlamydomonas reinhardtii in a flat capillary. Depending on the concentration of microswimmers, the translational and rotational diffusion constants increase by several orders of magnitude in the presence of the swimming algae. For low concentrations of algae, the doublets exhibit Brownian motion in a fluctuating flow field generated by multiple swimmers. One can observe strong, diffusive transport caused by occasional large displacements. At high swimmer concentration, the algae form dense clusters, where the rotational motion of the doublets shows a subdiffusive behaviour while the translational motion remains diffusive.

Swimming microorganisms can influence the diffusion of passive particles. The effect of this swimmer-particle interaction depends on different properties, such as the hydrodynamic field of the swimmer and the relative sizes of microorganisms and particles. We investigated an enhancement of the diffusion of silica doublets in a suspension of microalgae Chlamydomonas reinhardtii in a flat capillary. Depending on the concentration of microswimmers, the translational and rotational diffusion constants increase by several orders of magnitude in the presence of the swimming algae. For low concentrations of algae, the doublets exhibit Brownian motion in a fluctuating flow field generated by multiple swimmers. One can observe strong, diffusive transport caused by occasional large displacements. At high swimmer concentration, the algae form dense clusters, where the rotational motion of the doublets shows a subdiffusive behaviour while the translational motion remains diffusive.

Myofibrils in striated muscle cells are chains of regular cytoskeletal units termed sarcomeres, whose contractions drive voluntary movements of animals. Despite the well characterized order of the sarcomere components in mature sarcomeres, which explains the sarcomere contraction mechanism, the mechanism of molecular ordering during sarcomere assembly remains debated. Here, we put forward a theoretical framework for the self-assembly of sarcomeres. This theory is based on measurements of the sequential ordering of sarcomere components in developingDrosophilaflight muscles, identified by applying a novel tracking-free algorithm: myosin,α-actinin and the titin homologue Sallimus form periodic patterns before actin. Based on these results, we propose that myosin, Sallimus, and sarcomere Z-disc proteins includingα-actinin dynamically bind and unbind to an unordered bundle of actin filaments to establish an initial periodic pattern. As a consequence, periodicity of actin filaments is only established later. Our model proposes that non-local interactions between spatially extended myosin and titin/Sallimus containing complexes, and possibly tension-dependent feedback mediated by anα-actinin catch-bond, drive this ordering process. We probe this hypothesis using mathematical models and derive predictive conditions for sarcomere pattern formation, guiding future experimental analysis.