Biomolecular condensates sequester an aggregation-prone peptide and prevent its aggregation, showing that heterotypic interactions within the condensates can prevent the formation of amyloid fibrils, despite the local increase in concentration.
Spontaneous liquid demixing of biomolecules appears to be an efficient strategy developed by cells to organize reactions in space and time. This process allows cells to modulate biochemical reactions by locally changing the concentration and the environment of specific components. Here, we develop a strategy to couple the formation of biomolecular liquid compartments with reactions occuring within them. In particular, we conjugate a kinase enzyme with biologically derived low complexity domains and develop synthetic micro-reactors that locally increase the enzyme concentration up to 140-fold. We show that these micro-reactors are characterized by a polarity comparable to methanol which promotes recruitment of small molecules. Despite exhibiting higher viscosity with respect to the surrounding solution, the reactors are liquid-like and allow molecular diffusion within their interior. We demonstrate that the local increase in enzyme concentration accelerates the corresponding enzymatic rate up to 5-fold. This flexible strategy enables the generation of biomolecular microreactors with enhanced reactivity, with potential applications in heterogeneous biocatalysis.
The front cover artwork is provided by the Arosio Lab at ETH Zurich. The image shows liquid phase separated droplets that are based on biologically inspired intrinsically disordered proteins and act as microreactors for enhanced enzymatic reactions. Read the full text of the Article at 10.1002/syst.202000001. ChemSystemsChem
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