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A. Pasha Tabatabai

Publications and source records attributed to A. Pasha Tabatabai.

6 recordsLinked to original sources

Spatial Confinement Affects the Heterogeneity and Interactions Between Shoaling Fish

Living objects are able to consume chemical energy and process information independently from others. However, living objects can coordinate to form ordered groups such as schools of fish. This work considers these complex groups as living materials and presents imaging-based experiments of laboratory schools of fish to understand how this non-equilibrium activity affects the mechanical properties of a group. We use spatial confinement to control the motion and structure of fish within quasi-2D shoals of fish. Using image analysis techniques, we make quantitative observations of the structures, their spatial heterogeneity, and their temporal fluctuations. Furthermore, we utilize Monte Carlo simulations to replicate the experimentally observed area distribution patterns which provide insight into the effective interactions between fish and confirm the presence of a confinement-based behavioral preference transition. In addition, unlike in short-range interacting systems, here structural heterogeneity and dynamic activities are positively correlated as a result of complex interplay between spatial arrangement and behavioral dynamics in fish collectives.

cond-mat.soft↗

Non-reciprocal interactions spatially propagate fluctuations in a 2D Ising model

Motivated by the anisotropic interactions between fish, we implement spatially anisotropic and therefore non-reciprocal interactions in the 2D Ising model. First, we show that the model with non-reciprocal interactions alters the system critical temperature away from that of the traditional 2D Ising model. Further, local perturbations to the magnetization in this out-of-equilibrium system manifest themselves as traveling waves of spin states along the lattice, also seen in a mean-field model of our system. The speed and directionality of these traveling waves are controllable by the orientation and magnitude of the non-reciprocal interaction kernel as well as the proximity of the system to the critical temperature.

cond-mat.soft↗

Cooperation of dual modes of cell motility promotes epithelial stress relaxation to accelerate wound healing

Collective cell migration in cohesive units is vital for tissue morphogenesis, wound repair, and immune response. While the fundamental driving forces for collective cell motion stem from contractile and protrusive activities of individual cells, it remains unknown how their balance is optimized to maintain tissue cohesiveness and the fluidity for motion. Here we present a cell-based computational model for collective cell migration during wound healing that incorporates mechanochemical coupling of cell motion and adhesion kinetics with stochastic transformation of active motility forces. We show that a balance of protrusive motility and actomyosin contractility is optimized for accelerating the rate of wound repair, which is robust to variations in cell and substrate mechanical properties. This balance underlies rapid collective cell motion during wound healing, resulting from a tradeoff between tension mediated collective cell guidance and active stress relaxation in the tissue.

physics.bio-ph↗

Entropy Production Rate is Maximized in Non-Contractile Actomyosin

The actin cytoskeleton is an active semi-flexible polymer network whose non-equilibrium properties coordinate both stable and contractile behaviors to maintain or change cell shape. While myosin motors drive the actin cytoskeleton out-of-equilibrium, the role of myosin-driven active stresses in the accumulation and dissipation of mechanical energy is unclear. To investigate this, we synthesize an actomyosin material in vitro whose active stress content can tune the network from stable to contractile. Each increment in activity determines a characteristic spectrum of actin filament fluctuations which is used to calculate the total mechanical work and the production of entropy in the material. We find that the balance of work and entropy does not increase monotonically and, surprisingly, the entropy production rate is maximized in the non-contractile, stable state. Our study provides evidence that the origins of system entropy production and activity-dependent dissipation arise from disorder in the molecular interactions between actin and myosin

cond-mat.soft↗

Epithelial Wound Healing Coordinates Distinct Actin Network Architectures to Conserve Mechanical Work and Balance Power

How cells with diverse morphologies and cytoskeletal architectures modulate their mechanical behaviors to drive robust collective motion within tissues is poorly understood. During wound repair within epithelial monolayers in vitro, cells coordinate the assembly of branched and bundled actin networks to regulate the total mechanical work produced by collective cell motion. Using traction force microscopy, we show that the balance of actin network architectures optimizes the wound closure rate and the magnitude of the mechanical work. These values are constrained by the effective power exerted by the monolayer, which is conserved and independent of actin architectures. Using a cell-based physical model, we show that the rate at which mechanical work is done by the monolayer is limited by the transformation between actin network architectures and differential regulation of cell-substrate friction. These results and our proposed molecular mechanisms provide a robust quantitative model for how cells collectively coordinate their non-equilibrium behaviors to dynamically regulate tissue-scale mechanical output.

physics.bio-ph↗

Acid induced assembly of a reconstituted silk protein system

Silk cocoons are reconstituted into an aqueous suspension, and protein stability is investigated by comparing the protein's response to hydrochloric acid and sodium chloride. Aggregation occurs at <8 mM hydrochloric acid that is not correlated to protein protonation, while sodium chloride over the same range of concentrations does not cause aggregation. We measure the structures present on the protein and aggregate lengthscales in these solutions using both optical and neutron scattering, while mass spectrometry techniques shed light on a possible mechanism for aggregate formation. We find that the introduction of acid modulates the aggregate size and pervaded volume of the protein, an effect that is not observed with salt.

cond-mat.soft↗