Dresden 2026 – scientific programme
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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 45: Focus Session: Theoretical Modeling and Simulation of Biomolecular Condensates I (joint session CPP/BP)
CPP 45.6: Talk
Thursday, March 12, 2026, 11:00–11:15, ZEU/0260
Chemically driven simulations of enzymatic phosphorylation in protein condensates — •Emanuele Zippo1, Dorothee Dormann1,2, Thomas Speck3, and Lukas Stelzl1,2 — 1Johannes Gutenberg University Mainz, Mainz, Germany — 2Institute of Molecular Biology (IMB), Mainz, Germany — 3University of Stuttgart, Stuttgart, Germany
The condensation and aggregation of intrinsically disordered proteins (IDPs) in cells are governed by enzyme-driven, non-equilibrium processes. Kinases such as Casein kinase 1 delta (CK1d) phosphorylate proteins using ATP as chemical fuel, tuning intermolecular interactions and modulating condensate assembly. The neurodegeneration-linked protein TDP-43 undergoes CK1d-mediated hyperphosphorylation, proposed as a cytoprotective mechanism through condensate dissolution, yet the mechanisms underlying kinase-condensate interactions remain unclear. Using coarse-grained molecular dynamics simulations, we investigate how CK1d phosphorylates TDP-43 and how this reaction drives the structural reorganization and dissolution of its condensates. To ensure thermodynamic consistency in such fuel-driven simulations, we employ an automatic, generally applicable Markov state modeling framework. Post-translational modifications (PTMs), such as phosphorylation, can actively regulate condensate stability and suppress Ostwald ripening, offering a mechanism to control mesoscale structure in soft materials. Understanding such reaction-structure coupling in non-equilibrium environments is key to explaining cellular self-organization and designing biomimetic systems.
Keywords: molecular dynamics; protein; phase separation; phosphorylation; non-equilibrium