Non-equilibrium biomolecular condensates

FrontImage_ProteinSelfAssembly

Self-​assembly of biomolecules is crucial in both functional and dysfunctional biology. Protein aggregation and phase transition are increasingly associated with regulation of cellular functions in space and time, as well as with pathological conditions including Alzheimer’s and Parkinson’s disease. Since biological systems are out-​of-equilibrium, in addition to thermodynamics, kinetics is crucial to govern the behavior of the system. Proteins can access a variety of physical states, ranging from dynamic condensates to irreversible aggregates, which may be only metastable and under kinetic control. We apply traditional and modern tools of chemical reaction engineering, including microfluidics, to characterize the molecular determinants of the dynamics of condensates, focusing on two major problems: i) maturation of condensates into amyloid fibrils, and ii) material properties and aging of condensates of DEAD-box RNA binding proteins associated with cell compartmentalization and RNA metabolism.

Contacts

Condensates and amyloids: Chiara, Marcell, Lenka

Condensates and material properties: Charlotte, Timo, Kasia

Key publications

external page M. Linsenmeier et al. "Dynamic arrest and aging of biomolecular condensates are modulated by low-complexity domains, RNA and biochemical activity" Nature Communications, 2022.

external page M. Linsenmeier et al. "Dynamics of Synthetic Membraneless Organelles in Microfluidic Droplets" Angewandte Chemie Int. Ed., 2019.

external page M. Linsenmeier et al. "The interface of condensates of the hnRNPA1 low-complexity domain promotes formation of amyloid fibrils." Nat. Chem., 2023


 

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