- 【Updated on May 12, 2025】 Integration of CiNii Dissertations and CiNii Books into CiNii Research
- Trial version of CiNii Research Automatic Translation feature is available on CiNii Labs
- Suspension and deletion of data provided by Nikkei BP
- Regarding the recording of “Research Data” and “Evidence Data”
Vibrational spectroscopy analysis of ligand efficacy in human M₂ muscarinic acetylcholine receptor (M₂R)
-
- Katayama, Kota
- Department of Life Science and Applied Chemistry, Nagoya Institute of Technology; OptoBioTechnology Research Center, Nagoya Institute of Technology; PRESTO, Japan Science and Technology Agency
-
- Suzuki, Kohei
- Department of Life Science and Applied Chemistry, Nagoya Institute of Technology
-
- Suno, Ryoji
- Department of Medical Chemistry, Kansai Medical University
-
- Kise, Ryoji
- Graduate School of Pharmaceutical Sciences, Tohoku University
-
- Tsujimoto, Hirokazu
- Department of Cell Biology and Medical Chemistry, Graduate School of Medicine, Kyoto University
-
- Iwata, So
- Department of Cell Biology and Medical Chemistry, Graduate School of Medicine, Kyoto University
-
- Inoue, Asuka
- Graduate School of Pharmaceutical Sciences, Tohoku University
-
- Kobayashi, Takuya
- Department of Medical Chemistry, Kansai Medical University; Japan Agency for Medical Research and Development, Core Research for Evolutional Science and Technology (AMED-CREST)
-
- Kandori, Hideki
- Department of Life Science and Applied Chemistry, Nagoya Institute of Technology; OptoBioTechnology Research Center, Nagoya Institute of Technology
Description
The intrinsic efficacy of ligand binding to G protein-coupled receptors (GPCRs) reflects the ability of the ligand to differentially activate its receptor to cause a physiological effect. Here we use attenuated total reflection-Fourier transform infrared (ATR-FTIR) spectroscopy to examine the ligand-dependent conformational changes in the human M₂ muscarinic acetylcholine receptor (M₂R)). We show that different ligands affect conformational alteration appearing at the C=O stretch of amide-I band in M2R. Notably, ATR-FTIR signals strongly correlated with G-protein activation levels in cells. Together, we propose that amide-I band serves as an infrared probe to distinguish the ligand efficacy in M₂R) and paves the path to rationally design ligands with varied efficacy towards the target GPCR.
Journal
-
- Communications Biology
-
Communications Biology 4 1321-, 2021
Springer Nature
Related Articles
See more- Tweet
Details 詳細情報について
-
- CRID
- 1050290307570867968
-
- NII Article ID
- 120007173788
-
- ISSN
- 23993642
-
- HANDLE
- 2433/266295
-
- Text Lang
- en
-
- Article Type
- journal article
-
- Data Source
-
- IRDB
- Crossref
- CiNii Articles
- KAKEN
- OpenAIRE
