Chiral-filament self-assembly on curved manifolds
S Rode and J Elgeti and G Gompper, SOFT MATTER, 16, 10548-10557 (2020).
Rod-like and banana-shaped proteins, like BAR-domain proteins and MreB proteins, adsorb on membranes and regulate the membrane curvature. The formation of large filamentous complexes of these proteins plays an important role in cellular processes like membrane trafficking, cytokinesis and cell motion. We propose a simplified model to investigate such curvature-dependent self-assembly processes. Anisotropic building blocks, modeled as trimer molecules, which have a preferred binding site, interact via pair-wise Lennard-Jones potentials. When several trimers assemble, they form an elastic ribbon with an intrinsic curvature and twist, controlled by bending and torsional rigidity. For trimer self-assembly on the curved surface of a cylindrical membrane, this leads to a preferred spatial orientation of the ribbon. We show that these interactions can lead to the formation of helices with several windings around the cylinder. The emerging helix angle and pitch depend on the rigidities and the intrinsic curvature and twist values. In particular, a well-defined and controllable helix angle emerges in the case of equal bending and torsional rigidity. The dynamics of filament growth is characterized by three regimes, in which filament length increases with the power laws t(z) in time, with z similar or equal to 3/4, z = 1/2, and z = 0 for short, intermediate, and long times, respectively. A comparison with the solutions of the Smoluchowski aggregation equation allows the identification of the underlying mechanism in the short-time regime as a crossover from size- independent to diffusion-limited aggregation. Thus, helical structures, as often observed in biology, can arise by self-assembly of anisotropic and chiral proteins.
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