Light-induced assembly and repeatable actuation in Ca2+-driven chemomechanical protein networks
Year: 2026
Type: article
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 Ca 2+ -sensitive contractile protein. These networks—driven by Ca 2+ -triggered structural rearrangements—exhibit dynamic self-assembly, spatiotemporal growth, and contraction rates comparable to actomyosin systems. By coupling light-sensitive chelators for optically triggered Ca 2+ 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.
Source: Nature Communications
Language: English
Subfield: Mechanical Engineering
Field: Engineering
Domain: Physical Sciences
Open Access status: gold
Estimated APC paid: $6,990
Awards: Collaborative Research: Understanding and controlling force generation by a centrin-based contractile system, Collaborative Research: Understanding and controlling force generation by a centrin-based contractile system, Materials Research Science and Engineering Center, G4657484576, Collaborative Research: Understanding and controlling force generation by a centrin-based contractile system, Collaborative Research: Understanding and controlling force generation by a centrin-based contractile system, Biophysical mechanism and synthetic engineering of optically-controlled Ca2+-powered supramolecular engines
OpenAlex ID: W7130867291
