bioRxiv · 10.1101/2025.03.03.641304
Light-induced reversible assembly and actuation in ultrafast Ca2+-driven chemomechanical protein networks
Abstract
Programming rapid, repeatable motions in soft materials has remained a challenge in active matter and biomimetic design. Here, we present a light-controlled chemomechanical network based on Tetrahymena thermophila calcium-binding protein 2 (Tcb2), a Ca2+-sensitive contractile protein. These networks--driven by Ca2+-triggered structural rearrangements--exhibit dynamic selfassembly, spatiotemporal growth, and contraction rates comparable to actomyosin systems. By coupling light-sensitive chelators for optically triggered Ca2+ release, we achieve precise growth and repeatable mechanical contractility of Tcb2 networks, revealing emergent phenomena such as boundary-localized active regions and density gradient-driven reversals in motion. A coupled reaction-diffusion and elastic model explains these dynamics, highlighting the interplay between chemical network assembly and mechanical response. We further demonstrate active transport of particles via network-mediated forces in vitro and implement reinforcement learning to program seconds-scale spatiotemporal actuation in silico. These results establish a platform for designing responsive active materials with rapid chemomechanical dynamics and tunable optical control, with applications in synthetic cells, sub-cellular force generation, and programmable biomaterials.
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Lei, X., Floyd, C., Ferrer, L. C., Chakrabortty, T., Chandrasekharan, N., Dinner, A., Coyle, S. M., Honts, J., Bhamla, S.. 2025-03-12. Light-induced reversible assembly and actuation in ultrafast Ca2+-driven chemomechanical protein networks. https://doi.org/10.1101/2025.03.03.641304
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