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A synthetic ion channel with anisotropic ligand response

Author

Listed:
  • Takahiro Muraoka

    (Tokyo Institute of Technology
    Japan Science and Technology Agency)

  • Daiki Noguchi

    (Tohoku University)

  • Rinshi S. Kasai

    (Kyoto University, Shougoin)

  • Kohei Sato

    (Tokyo Institute of Technology)

  • Ryo Sasaki

    (Tokyo Institute of Technology)

  • Kazuhito V. Tabata

    (The University of Tokyo, Bunkyo-ku)

  • Toru Ekimoto

    (Yokohama City University)

  • Mitsunori Ikeguchi

    (Yokohama City University
    Medical Sciences Innovation Hub Program RIKEN)

  • Kiyoto Kamagata

    (Tohoku University)

  • Norihisa Hoshino

    (Tohoku University)

  • Hiroyuki Noji

    (The University of Tokyo, Bunkyo-ku)

  • Tomoyuki Akutagawa

    (Tohoku University)

  • Kazuaki Ichimura

    (Tokyo Institute of Technology)

  • Kazushi Kinbara

    (Tokyo Institute of Technology
    Tohoku University)

Abstract

Biological membranes play pivotal roles in the cellular activities. Transmembrane proteins are the central molecules that conduct membrane-mediated biochemical functions such as signal transduction and substance transportation. Not only the molecular functions but also the supramolecular properties of the transmembrane proteins such as self-assembly, delocalization, orientation and signal response are essential for controlling cellular activities. Here we report anisotropic ligand responses of a synthetic multipass transmembrane ion channel. An unsymmetrical molecular structure allows for oriented insertion of the synthetic amphiphile to a bilayer by addition to a pre-formed membrane. Complexation with a ligand prompts ion transportation by forming a supramolecular channel, and removal of the ligand deactivates the transportation function. Biomimetic regulation of the synthetic channel by agonistic and antagonistic ligands is also demonstrated not only in an artificial membrane but also in a biological membrane of a living cell.

Suggested Citation

  • Takahiro Muraoka & Daiki Noguchi & Rinshi S. Kasai & Kohei Sato & Ryo Sasaki & Kazuhito V. Tabata & Toru Ekimoto & Mitsunori Ikeguchi & Kiyoto Kamagata & Norihisa Hoshino & Hiroyuki Noji & Tomoyuki Ak, 2020. "A synthetic ion channel with anisotropic ligand response," Nature Communications, Nature, vol. 11(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16770-z
    DOI: 10.1038/s41467-020-16770-z
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    Cited by:

    1. Jae-Hyun Park & Kouki Kawakami & Naito Ishimoto & Tatsuya Ikuta & Mio Ohki & Toru Ekimoto & Mitsunori Ikeguchi & Dong-Sun Lee & Young-Ho Lee & Jeremy R. H. Tame & Asuka Inoue & Sam-Yong Park, 2023. "Structural basis for ligand recognition and signaling of hydroxy-carboxylic acid receptor 2," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Zhikuan Zhang & Norimichi Nomura & Yukiko Muramoto & Toru Ekimoto & Tomoko Uemura & Kehong Liu & Moeko Yui & Nozomu Kono & Junken Aoki & Mitsunori Ikeguchi & Takeshi Noda & So Iwata & Umeharu Ohto & T, 2022. "Structure of SARS-CoV-2 membrane protein essential for virus assembly," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    3. Jie Shen & Yongting Gu & Lingjie Ke & Qiuping Zhang & Yin Cao & Yuchao Lin & Zhen Wu & Caisheng Wu & Yuguang Mu & Yun-Long Wu & Changliang Ren & Huaqiang Zeng, 2022. "Cholesterol-stabilized membrane-active nanopores with anticancer activities," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    4. Swarup Dey & Adam Dorey & Leeza Abraham & Yongzheng Xing & Irene Zhang & Fei Zhang & Stefan Howorka & Hao Yan, 2022. "A reversibly gated protein-transporting membrane channel made of DNA," Nature Communications, Nature, vol. 13(1), pages 1-12, December.

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