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Register a new userGeometrical frustration yields fiber formation in self-assembly
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Controlling the self-assembly of supramolecular structures is vital for living cells, and a central challenge for engineering at the nano- and microscales. Nevertheless, even particles without optimized shapes can robustly form well-defined morphologies. This is the case in numerous medical conditions where normally soluble proteins aggregate into fibers. Beyond the diversity of molecular mechanisms involved, we propose that fibers generically arise from the aggregation of irregular particles with short-range interactions. Using a minimal model of ill-fitting, sticky particles, we demonstrate robust fiber formation for a variety of particle shapes and aggregation conditions. Geometrical frustration plays a crucial role in this process, and accounts for the range of parameters in which fibers form as well as for their metastable character.
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Protein aggregation in the form of amyloid fibrils has important biological and technological implications. Although the self-assembly process is highly efficient, aggregates not in the fibrillar form would also occur and it is important to include these disordered species when discussing the thermodynamic equilibrium behavior of the system. Here, we initiate such a task by considering a mixture of monomeric proteins and the corresponding aggregates in the disordered form (micelles) and in the fibrillar form (amyloid fibrils). Starting with a model on the respective binding free energies for these species, we calculate their concentrations at thermal equilibrium. We then discuss how the incorporation of the disordered structure furthers our understanding on the various amyloid promoting factors observed empirically, and on the kinetics of fibrilization.
Elongation is a fundament process in amyloid fiber growth, which is normally characterized by a linear relationship between the fiber elongation rate and the monomer concentration. However, in high concentration regions, a sub-linear dependence was often observed, which could be explained by a universal saturation mechanism. In this paper, we modeled the saturated elongation process through a Michaelis-Menten like mechanism, which is constituted by two sub-steps -- unspecific association and dissociation of a monomer with the fibril end, and subsequent conformational change of the associated monomer to fit itself to the fibrillar structure. Typical saturation concentrations were found to be $7-70mu M$ for A$beta$40, $alpha$-synuclein and etc. Furthermore, by using a novel Hamiltonian formulation, analytical solutions valid for both weak and strong saturated conditions were constructed and applied to the fibrillation kinetics of $alpha$-synuclein and silk fibroin.
External control of the swimming speed of `active particles can be used to self assemble designer structures in situ on the micrometer to millimeter scale. We demonstrate such reconfigurable templated active self assembly in a fluid environment using light powered strains of Escherichia coli. The physics and biology controlling the sharpness and formation speed of patterns is investigated using a bespoke fast-responding strain.
Filamentous bacteriophages such as fd-like viruses are monodisperse rod-like colloids that have well defined properties: diameter, length, rigidity, charge and chirality. Engineering those viruses leads to a library of colloidal rods which can be used as building blocks for reconfigurable and hierarchical self-assembly. Their condensation in aqueous solution th{with additive polymers which act as depletants to induce} attraction between the rods leads to a myriad of fluid-like micronic structures ranging from isotropic/nematic droplets, colloid membranes, achiral membrane seeds, twisted ribbons, $pi$-wall, pores, colloidal skyrmions, Mobius anchors, scallop membranes to membrane rafts. Those structures and the way they shape shift not only shed light on the role of entropy, chiral frustration and topology in soft matter but it also mimics many structures encountered in different fields of science. On one hand, filamentous phages being an experimental realization of colloidal hard rods, their condensation mediated by depletion interactions constitutes a blueprint for self-assembly of rod-like particles and provides fundamental foundation for bio- or material oriented applications. On the other hand, the chiral properties of the viruses restrict the generalities of some results but vastly broaden the self-assembly possibilities.
The smallest maximum kissing-number Voronoi polyhedron of 3d spheres is the icosahedron and the tetrahedron is the smallest volume that can show up in Delaunay tessalation. No periodic lattice is consistent with either and hence these dense packings are geometrically frustrated. Because icosahedra can be assembled from almost perfect tetrahedra, the terms icosahedral and polytetrahedral packing are often used interchangeably, which leaves the true origin of geometric frustration unclear. Here we report a computational study of freezing of 4d hard spheres, where the densest Voronoi cluster is compatible with the symmetry of the densest crystal, while polytetrahedral order is not. We observe that, under otherwise comparable conditions, crystal nucleation in 4d is less facile than in 3d. This suggest that it is the geometrical frustration of polytetrahedral structures that inhibits crystallization.
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