The accuracy and the fidelity of a single-molecule force measurement largely rely on how the molecule of interest is attached to the solid substrate surface (bead, cantilever, cover glass and etc.). A site-specific attachment of a protein without affecting its structure and enzymatic function has been a major concern. Here, we established a glutathione-coupled cantilever to which any glutathione S-transferase (GST)-fused proteins can be attached in a desired direction. The rupture force between glutathione and GST was ∼100 pN on average. By using this cantilever, we succeeded in measuring the interaction force between importin α and importin β. © 2006.
Yoshimura, S. H., Takahashi, H., Otsuka, S., & Takeyasu, K. (2006). Development of glutathione-coupled cantilever for the single-molecule force measurement by scanning force microscopy. FEBS Letters, 580(16), 3961–3965. https://doi.org/10.1016/j.febslet.2006.06.032