July 18, 2022 -- Researchers from the University of Wisconsin-Milwaukee have built a tool to investigate the mechanical response of the R8 rod domain of talin. They found under various force cycles, the R8 domain of talin can display a memory-dependent behavior. In response to an applied force, talin unfolds and refolds, forming a structure where the ligand DCL1 binds almost irreversibly.
Using "single molecule magnetic tweezers," the researchers measured intracellular mechanical forces (< 10 pN) and experimented with them in the lab so they could determine what happens to talin when DCL1 is both present and not present in the cell (Science Advances, July 15, 2022).
They found a unique behavior of talin that shows a strong interaction and can explain the antitumor effect of DLC1 when the two proteins bind. Using the magnetic tweezers, the team tethered a protein molecule between a glass surface and a paramagnetic bead. They measured the position of the paramagnetic bead at a freely moving end of the molecule as well as the nonmagnetic bead. Both beads were glued to the same surface but opposite the protein. After applying a magnetic force and replicating the exact mechanical perturbations a protein endures, the researchers measured talin's unfolding and refolding over the course of days.
More research on the protein interaction could be used to develop cancer drugs, the researchers concluded.
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