2024-03-28T15:51:05Z
https://tsukuba.repo.nii.ac.jp/oai
oai:tsukuba.repo.nii.ac.jp:00038712
2022-04-27T09:08:37Z
117:1443
29:297
3:62:5297:1814
Analysis of the aplyronine A-induced protein-protein interaction between actin and tubulin by surface plasmon resonance
木越, 英夫
北, 将樹
Hirayama, Yuichiro
Yamagishi, Kota
Suzuki, Tomohiro
Kawagishi, Hirokazu
Kita, Masaki
木越, 英夫
キゴシ, ヒデオ
© 2016. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
The antitumor macrolide aplyronine A induces protein–protein interaction (PPI) between actin and tubu-lin to exert highly potent biological activities. The interactions and binding kinetics of these molecules were analyzed by the surface plasmon resonance with biotinylated aplyronines or tubulin as ligands.
Strong binding was observed for tubulin and actin with immobilized aplyronine A. These PPIs were almost completely inhibited by one equivalent of either aplyronine A or C, or mycalolide B. In contrast,
a non-competitive actin-depolymerizing agent, latrunculin A, highly accelerated their association.
Significant binding was also observed for immobilized tubulin with an actin–aplyronine A complex,
and the dissociation constant K D was 1.84 l M. Our method could be used for the quantitative analysis of the PPIs between two polymerizing proteins stabilized with small agents.
Elsevier
2016-06
eng
journal article
http://hdl.handle.net/2241/00143388
https://tsukuba.repo.nii.ac.jp/records/38712
27161875
10.1016/j.bmc.2016.04.049
0968-0896
AA10938083
Bioorganic & medicinal chemistry
24
12
2809
2814
https://tsukuba.repo.nii.ac.jp/record/38712/files/BMC_24-12.pdf
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747.2 kB
2018-07-01