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Colloidal systems possess unique features to investigate the governing principles behind liquid-to-solid transitions. The phase diagram and crystallization landscape of colloidal particles can be finely tuned by the range, number and angular distribution of attractive interactions between the constituent particles. In this work, we present a computational study of colloidal patchy particles with high-symmetry bonding—six patches displaying octahedral symmetry—that can crystallize into distinct competing ordered phases: a cubic simple (CS) lattice, a body-centered cubic (BCC) phase, and two face-centered cubic (FCC) solids (orientationally ordered and disordered). We investigate the underlying mechanisms by which these competing crystals emerge from a disordered fluid at different pressures. Strikingly, we identify instances where the structure of the crystalline embryo corresponds to the stable solid, while in others it corresponds to a metastable crystal whose nucleation is enabled by its lower interfacial free energy with the liquid. Moreover, we find the exceptional phenomenon that, due to a subtle balance between volumetric enthalpy and interfacial free energy, the CS phase nucleates via crystalline cubic nuclei rather than through spherical clusters as the majority of crystal solids in nature. Finally, by examining growth beyond the nucleation stage, we uncover a series of alternating one-phase and two-phase crystallization mechanisms, depending on whether or not the same phase that nucleates keeps growing. Taken together, we show that an octahedral distribution of attractive sites in colloidal particles results in an extremely rich crystallization landscape where subtle differences in pressure crucially determine the crystallizing polymorph.

Maturation of functional liquid-like biomolecular condensates into solid-like aggregates has been linked to the onset of several neurodegenerative disorders. Low-complexity aromatic-rich kinked segments (LARKS) contained in numerous RNA-binding proteins can promote aggregation by forming inter-proteinβ-sheet fibrils that accumulate over time and ultimately drive the liquid-to-solid transition of the condensates. Here, we combine atomistic molecular dynamics simulations with sequence-dependent coarse-grained models of various resolutions to investigate the role of LARKS abundance and position within the amino acid sequence in the maturation of condensates. Remarkably, proteins with tail-located LARKS display much higher viscosity over time than those in which the LARKS are placed towards the center. Yet, at very long timescales, proteins with a single LARKS—independently of its location—can still relax and behave as high viscous liquids. However, phase-separated condensates of proteins containing two or more LARKS become kinetically trapped due to the formation of percolatedβ-sheet networks that display gel-like behaviour. Furthermore, as a work case example, we demonstrate how shifting the location of the LARKS-containing low-complexity domain of FUS protein towards its center effectively precludes the accumulation ofβ-sheet fibrils in FUS-RNA condensates, maintaining functional liquid-like behaviour without ageing.