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Biology subjects

Sada, K.

Publications and source records attributed to Sada, K..

3 recordsLinked to original sources

Force Scaling in Active Swarm of Microtubules via Magnetic Manipulation

Scalability refers to the ability of a system to enhance performance with increasing size. This ability is a defining feature of natural swarms such as ant and bee colonies. Extending this principle to artificial active matter has motivated the creation of molecular swarms composed of myosin-driven actin filaments and kinesin-driven microtubules (MTs). While these swarms exhibit cooperative transport behaviors that surpass the abilities of individual filaments, their collective force generation has remained unquantified. Here, we introduce a straightforward electromagnetic tweezer approach to directly measure the forces generated by MT swarms propelled by surface-bound kinesin motors. We find that force output changes with swarm size, demonstrating quantitative scalability and linking collective organization to mechanical performance. These results establish MT swarms as a model system for scalable, force-producing active matter and provide a foundation for designing biomolecular devices that exploit collective dynamics for microscale actuation and transport. Significance StatementThe cooperative activity of multiple motile agents is observed in nature, known as swarming. In artificial systems, swarming has been demonstrated using active agents like kinesin and MTs, successfully enabling efficient cargo transportation. However, the force generated by the swarm remains unexplored, which is one of the keys to understanding the principles underlying swarm systems. This study introduces a simple method employing electromagnetic tweezers and magnetic beads to measure the force of the MT swarm accurately. The measured forces within the microtubule swarms of different sizes unveil the scaling effect, the additive nature of force generation as the kinesin unit increases. The force study sheds light on the fundamental properties, work performance, efficiency, and execution of the MT swarm.

biophysics↗

Generation of stable microtubule superstructures by binding of peptide-fused tetrameric proteins to inside and outside

Microtubules (MTs) play important roles in biological functions by forming superstructures, such as doublets, triplets, and branched structures, in vivo. Formation of these superstructures by exogenous molecules in vitro will be useful not only for understanding the functions of MTs but also as components of MT-based nanomaterials. Here, we developed a tetrameric fluorescent protein Azami-Green (AG) fused with a His-tag and Tau-derived peptide (TP), TP-AG, which can bind to the inside or outside of MTs depending on the polymerization conditions. The binding of TP-AG to the inside of MTs induced the formation, stabilized, and increased the rigidity of the MTs. The binding of TP-AG to the outside of MTs induced various types of MT superstructures, including doublets, multiplets, and branched structures, by recruiting tubulins to MTs. The formation of motile MT aster structures by TP-AG was also observed. The generation of MT superstructures by these exogenous proteins provides guidelines for the design of MT-based nanomaterials.

bioengineering↗

TMAO regulates the rigidity of kinesin-propelled microtubules

We demonstrate that the rigidity of the microtubules (MTs), propelled by kinesins in an in vitro gliding assay, can be modulated using the deep-sea osmolyte trimethylamine N-oxide (TMAO). By varying the concentration of TMAO in the gliding assay, the rigidity of the MTs is modulated over a wide range. By employing this approach, we are able to reduce the persistence length of MTs, a measure of MT rigidity, [~]8 fold using TMAO of the concentration of 1.5 M. The rigidity of gliding MTs can be restored by eliminating the TMAO from the gliding assay. This work offers a simple strategy to regulate the rigidity of kinesin-propelled MTs in situ and would widen the applications of biomolecular motors in nanotechnology, materials science, and bioengineering.

biophysics↗