title: Trapping, entrainment and synchronization of semiflexible polymers in narrow, asymmetric confinements.
abstract: The physical properties of polymeric actin facilitate many mechanical processes within the cell, including cellular deformation and locomotion, whereby the polymers can be confined to a range of different geometries. As actin polymers often form entangled solutions in the cell, we have investigated the effect of confinement on the evolution of entangled semiflexible polymer solutions. Using a microfluidic platform, we examined the physical dynamics of actin polymers confined within narrow (2-4 μm) rectangular channels. Focusing on the entanglement process of two actin polymers, we found that their prolonged entrainment leads to synchronized horizontal undulations and decreased translational diffusion. In the absence of cross-linking molecules or proteins, the long-range entrainment interactions are predominantly controlled by the geometric boundaries. We directly measure the deflection length Λ for an individual polymer, either solitarily confined within a channel or confined in the presence of a second filament, enabling the determination of the change in free energy associated with polymer entanglement. Our results indicate that geometrical confinement can serve as a solitary variable influencing the physical dynamics of entangled semiflexible polymers.
authors.affiliation: Department of Chemistry, University of Basel, 4056 Basel, Switzerland. thomas.pfohl@unibas.ch.
authors.forename: Zoe
authors.initials: Z
authors.lastname: Swank
authors.affiliation: Department of Chemistry, University of Basel, 4056 Basel, Switzerland. thomas.pfohl@unibas.ch.
authors.forename: Siddharth
authors.initials: S
authors.lastname: Deshpande
authors.affiliation: Department of Chemistry, University of Basel, 4056 Basel, Switzerland. thomas.pfohl@unibas.ch.
authors.forename: Thomas
authors.initials: T
authors.lastname: Pfohl
mesh_terms: D008841:Actin Cytoskeleton / Q000737:chemistry*; D044085:Microfluidics; D056004:Molecular Dynamics Simulation; D011487:Protein Conformation