HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Research Institute for Electronic Science >
Peer-reviewed Journal Articles, etc >

Dynamic Control of Microbial Movement by Photoswitchable ATP Antagonists

Files in This Item:
ESI_Chem Sci_March 8 final.pdfElectronic Supplementary Information1.68 MBPDFView/Open
MS_Chem Sci_2022_March 8 final.pdf1.19 MBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/89537

Title: Dynamic Control of Microbial Movement by Photoswitchable ATP Antagonists
Authors: Thayyil, Sampreeth Browse this author
Nishigami, Yukinori Browse this author
Islam, Md Jahirul Browse this author
Hashim, P. K. Browse this author
Furuta, Ken'ya Browse this author
Oiwa, Kazuhiro Browse this author
Yu, Jian Browse this author
Yao, Min Browse this author
Nakagaki, Toshiyuki Browse this author
Tamaoki, Nobuyuki Browse this author →KAKEN DB
Keywords: azobenzene
ATP antagonist
dynein
motor protein
photocontrol
Issue Date: 25-May-2022
Publisher: Wiley-Blackwell
Journal Title: Chemistry-A European journal
Volume: 28
Issue: 30
Start Page: e202200807
Publisher DOI: 10.1002/chem.202200807
Abstract: 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.
Rights: 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.
Type: article (author version)
URI: http://hdl.handle.net/2115/89537
Appears in Collections:電子科学研究所 (Research Institute for Electronic Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 玉置 信之

Export metadata:

OAI-PMH ( junii2 , jpcoar_1.0 )

MathJax is now OFF:


 

 - Hokkaido University