Uncovering the thermodynamic principles of enzymaticregulation in biomolecular condensates with reactivesimulations
Lavagna, E.; Delfino, F.; Koniukov, G.; Paloni, M.; Ciandrini, L.; Barducci, A.
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Biomolecular condensates are dynamic cellular assemblies often regulated by energy-consuming processes such as post-translational modifications (PTMs). These reactions can act as molecular switches that control condensate assembly and dissolution, or sustain non-equilibrium steady states that support biological function. Nevertheless, how reaction dynamics couple to spatial organization at the molecular scale remains poorly understood. Here, we introduce a minimal molecular model to study enzymatic regulation of condensate assembly and structure under thermodynamic constraints. Our simulations reveal a non-monotonic dependence of condensate stability on modification strength, identifying an optimal regime for active control. We further find that chemical activity becomes spatially localized at the condensate interface, which emerges as a key reactive hub shaped by local molecular environments. Together, these results show how thermodynamically consistent, particle-based simulations can provide insight into principles of active condensate regulation at molecular resolution.
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