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Feigeles, C. A.

Publications and source records attributed to Feigeles, C. A..

2 recordsLinked to original sources

Capillary-induced bundling of biopolymer networks via protein condensates

Within the cell, biopolymers form self-organized assemblies that regulate cellular processes. These assemblies can be constructed through either protein interactions or phase separation. It is known that actin filaments, which form the mechanical structure of cells, are assembled into networks and bundles by protein cross-linkers. Different network and bundle microstructures support different physiological functions. Recently, there is evidence that protein condensates interact with biopolymers to create bundles. Here, we show that protein condensates colocalize with actin filaments and form networks of bundles. The condensates absorb on actin bundles and relax into a barrel shaped droplet on bundles, evocative of drops of simple liquids on fibers. We investigate the condensate spreading and measure contact angle that condensates make with bundles. Condensates at the intersection of bundles cause capillary bridges which induce network remodeling. Our results suggest that network formation, bundling, and remodeling in biopolymer assemblies could be induced by capillary interactions due to condensates. Understanding this bundling mechanism could expand our toolkit for making self-assembled fiber-based soft materials.

biophysics↗

Tuning the contractility and deformation modes of active actin-based assemblies in vitro: from 2D active networks to liquid crystal drops

Actin cytoskeleton-based materials are widely investigated as model cellular materials to elucidate physical mechanisms of cell mechanics, such as shape regulation and force production, as well as intriguing soft polymeric materials. In this method, we detail creating actin-based assemblies in vitro using purified protein for fluorescence microscopy studies. We polymerize long actin filaments in a sample chamber and use a polymer depletant to crowd filaments into a 2D-entangled network against a surface passivated with a surfactant layer. Adding skeletal muscle myosin II filaments in the presence of ATP induces contraction of the actin network. By bundling actin filaments with cross-linker, we tune the contractility of the assembly, transitioning from a material that buckles to a material that slides at the microscale. By reducing the length of the actin filaments through co-polymerizing actin in the presence of capping protein, we tune the material from being a 2D network to a liquid crystal. Cross-linking of dispersed short actin filaments results in 3D liquid crystal droplet formation.

biophysics↗