Dynamic Control of Microbial Movement by Photoswitchable ATP Antagonists

Thayyil, Sampreeth; Nishigami, Yukinori; Islam, Md Jahirul; Hashim, P. K.; Furuta, Ken'ya; Oiwa, Kazuhiro; Yu, Jian; Yao, Min; Nakagaki, Toshiyuki; Tamaoki, Nobuyuki

Dynamic Control of Microbial Movement by Photoswitchable ATP Antagonists

Thayyil, Sampreeth; Nishigami, Yukinori; Islam, Md Jahirul et al.

Chemistry-A European journal, 2022, 28(30), e202200807

Permalink : https://hdl.handle.net/2115/89537

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論文情報

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アクセス権	open access
URI	https://hdl.handle.net/2115/89537
タイトル	Dynamic Control of Microbial Movement by Photoswitchable ATP Antagonists
著者	Thayyil, Sampreeth ; Nishigami, Yukinori ; Islam, Md Jahirul ; Hashim, P. K. ; Furuta, Ken'ya ; Oiwa, Kazuhiro ; Yu, Jian ; Yao, Min ; Nakagaki, Toshiyuki ; Tamaoki, Nobuyuki
著者名 Thayyil, Sampreeth
著者名 Nishigami, Yukinori
著者名 Islam, Md Jahirul
著者名 Hashim, P. K.
著者名 Furuta, Ken'ya
著者名 Oiwa, Kazuhiro
著者名 Yu, Jian
著者名 Yao, Min
著者名 Nakagaki, Toshiyuki
e-Rad_Researcher 00344218 著者名 Tamaoki, Nobuyuki
言語	英語
キーワード	azobenzene
	ATP antagonist
	dynein
	motor protein
	photocontrol
発行日	2022-05-25
出版者	Wiley-Blackwell
収録物名	Chemistry-A European journal
巻(号)	28(30)
ページ	e202200807
抄録	Adenosine triphosphate (ATP) is the energy source for various biochemical processes and biomolecular motors in living things. Development of ATP antagonists and their stimuli-controlled actions offer a novel approach to regulate biological processes. Herein, we developed azobenzene-based photoswitchable ATP antagonists for controlling the activity of motor proteins; cytoplasmic and axonemal dyneins. The new ATP antagonists showed reversible photoswitching of cytoplasmic dynein activity in an in vitro dynein-microtubule system due to the trans and cis photoisomerization of their azobenzene segment. Importantly, our ATP antagonists reversibly regulated the axonemal dynein motor activity for the force generation in a demembranated model of Chlamydomonas reinhardtii. We found that the trans and cis isomers of ATP antagonists significantly differ in their affinity to the ATP binding site.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
権利情報	This is the peer reviewed version of the following article: [S. Thayyil, Y. Nishigami, M. J. Islam, P. K. Hashim, K.'y. Furuta, K. Oiwa, J. Yu, M. Yao, T. Nakagaki, N. Tamaoki, Chem. Eur. J. 2022, 28, e202200807.], which has been published in final form at [https://doi.org/10.1002/chem.202200807]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. This article may not be enhanced, enriched or otherwise transformed into a derivative work, without express permission from Wiley or by statutory rights under applicable legislation. Copyright notices must not be removed, obscured or modified. The article must be linked to Wiley’s version of record on Wiley Online Library and any embedding, framing or otherwise making available the article or pages thereof by third parties from platforms, services and websites other than Wiley Online Library must be prohibited.
PISSN	0947-6539
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1002/chem.202200807