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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 55: Focus Session: Theoretical Modeling and Simulation of Biomolecular Condensates III (joint session CPP/BP)
CPP 55.6: Vortrag
Freitag, 13. März 2026, 11:00–11:15, ZEU/0260
Biomolecular condensates with a Twist: From Assembly to Arrest — •Mahesh Yadav1,2 and Lukas Stelzl2 — 1Institute of Physics, Johannes Gutenberg University, Mainz — 2Institute of Molecular Physiology, Johannes Gutenberg University, Mainz
In this work, we investigate the phase behavior of RNA-binding protein Fused in Sarcoma (FUS), whose multivalent and intrinsically disordered regions drive the formation of biomolecular condensates through liquid-liquid phase separation. FUS is a multi-domain protein with arginine-glycine-rich segments (RG-rich domains) that participate in essential cellular proceses. We examine how characteristic sequence motifs such as RGG.. mediate homotypic and nucleic acid binding, and how targeted point mutations (e.g., RtoK, RtoA) disrupt these motifs and impair condensate formation. Using the thermodynamics phase diagram as a benchmark we highlighted the shift in phase separation propensity of the FUS and its variants. Furthermore, we identify the role of key interactions such as electrostatics, π-π and cation-π in nucleic acid binding at atomistic scale. We further characterized the emergent viscoelastic behavior of FUS condensates at multiple scales. We observe that upon mutations the overall dynamics slows down which reflects the gel-like state. Within the condensate interior, protein chains exhibit sub-diffusive dynamics arising from intermittent binding and viscoelastic resistance, mobility at the interface is further suppressed due to anisotropic interactions and interfacial confinement. To quantify these behaviors across relevant scales, we employ multi-resolution simulation models.
Keywords: Biomolecular condensates; phase behavior; Fused in Sarcoma; liquid-liquid phase sep- aration; viscoelastic behavior