Stabilization of microtubules by cevipabulin

  • Biochem Biophys Res Commun. 2019 Aug 27;516(3):760-764. doi: 10.1016/j.bbrc.2019.06.095.
Syeda Rubaiya Nasrin  1 Arif Md Rashedul Kabir  2 Akihiko Konagaya  3 Tsukasa Ishihara  4 Kazuki Sada  5 Akira Kakugo  6
Affiliations
  • 1. Graduate School of Chemical Sciences and Engineering, Hokkaido University, Sapporo, 060-0810, Hokkaido, Japan.
  • 2. Faculty of Science, Hokkaido University, Sapporo, 060-0810, Hokkaido, Japan.
  • 3. Department of Computational Intelligence and Systems Science, Tokyo Institute of Technology, Yokohama, 226-8502, Japan.
  • 4. Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, 305-8566, Japan.
  • 5. Graduate School of Chemical Sciences and Engineering, Hokkaido University, Sapporo, 060-0810, Hokkaido, Japan; Faculty of Science, Hokkaido University, Sapporo, 060-0810, Hokkaido, Japan.
  • 6. Graduate School of Chemical Sciences and Engineering, Hokkaido University, Sapporo, 060-0810, Hokkaido, Japan; Faculty of Science, Hokkaido University, Sapporo, 060-0810, Hokkaido, Japan. Electronic address: [email protected].
Abstract

We report the utility of cevipabulin as a stabilizing agent for microtubules. Cevipabulin-stabilized microtubules were more flexible compared to the microtubules stabilized by paclitaxel, the most commonly used microtubule stabilizing agent. Similar to the paclitaxel-stabilized microtubules, cevipabulin-stabilized microtubules were driven by kinesins in an in vitro gliding assay. The velocity of cevipabulin-stabilized microtubules was significantly higher than that of paclitaxel-stabilized microtubules. These findings will enrich the variety of microtubules with difference in mechanical and dynamic properties and widen their applications in nanotechnology.

Keywords
Cevipabulin; Kinesin; Microtubule; Motility assay; Persistence length.
Products