Skip to content
DraconiticResearch
Search Sources API
203,234 studies31 sourcesUpdated 49 min ago
Peer-reviewedCC BY-NC-NDThe journal of physical chemistry letters

High-Speed Atomic Force Microscopy Reveals Single-Molecule Dynamics of Fulvestrant-Bound Estrogen Receptor α.

  • Reon Imakawa1
  • Kota Aramaki2
  • Takeru Kajiyama2
  • Kota Yoshimura1
  • Towa Onohara2
  • Keesiang Lim3
  • Richard W Wong1,3,4
  • Ayami Matsushima2,5
5 affiliations
  1. 1Division of Nano Life Science in the Graduate School of Frontier Science Initiative, Kanazawa University, Kanazawa, Ishikawa920-1192, Japan.
  2. 2Laboratory of Structure-Function Biochemistry, Department of Chemistry, Graduate School of Science, Kyushu University, Fukuoka819-0395, Japan.
  3. 3WPI-Nano Life Science Institute, Kanazawa University, Kanazawa, Ishikawa, 920-1192, Japan.
  4. 4Cell-Bionomics Research Unit, Institute for Frontier Science Initiative (INFINITI), Kanazawa University, Kanazawa, Ishikawa920-1192, Japan.
  5. 5Laboratory of Structure-Function Biochemistry, Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka819-0395, Japan.
Read full textPDFDOICite

Abstract

Fulvestrant is a selective estrogen receptor downregulator (SERD) that antagonizes estrogen receptor α (ERα) and also promotes receptor degradation. However, how it affects full-length ERα dynamics at the single-molecule level remains unclear. Here, we used high-speed atomic force microscopy (HS-AFM) to directly visualize the dynamic behavior of full-length ERα under fulvestrant-bound, ligand-free, and other ligand-bound conditions. Among the four conditions, fulvestrant-bound ERα alone showed a reduced apparent molecular volume and increased surface mobility, behaving distinctly from the ligand-free, E2-bound, and 4-OHT-bound states. These results indicate that fulvestrant not only drives ERα inactivation and degradation but also is associated with changes in the observed molecular morphology and dynamics of full-length ERα. Our study provides direct single-molecule observation of altered molecular behavior under fulvestrant-bound conditions, which we interpret as reflecting changes in the conformational ensemble of full-length ERα.

Related

  1. A doubly charmed strange molecule from coupled-channel dynamics
    Hee-Jin Kim, Hyun-Chul Kim
    arXivPreprintarXiv licenceFull textHigh-energy & particle physicsarXiv
  2. Sequential Multistep Nanoimprint Lithography Fabrication of Zero-Mode Waveguide Nanoaperture Arrays to Enhance Single-Molecule Fluorescence Detection
    Hamza Khelidj, Badre Kerzabi, Igor Ozerov +3
    ACS photonicsPeer-reviewedLicence not statedCondensed matterOptics & photonicsHAL
  3. Improved Threshold for Particle-Induced Magnetic Avalanche in Single-Molecule Magnets Using Fe8 Molecule
    Bailey Kohn, Rupak Mahapatra, Ivan Borzenets +6
    arXivPreprintarXiv licenceFull textHigh-energy & particle physicsarXiv
  4. Depth estimation in fluorescence microscopy using degree of polarization
    Mingyang Xu, Naru Yoneda, Osamu Matoba
    Optics ExpressPeer-reviewedPublisher termsOptics & photonicsCrossref
  5. Inverse heterodyne effect in bimodal Kelvin probe force microscopy
    Hugo Valloire, Sylvain Clair, Christian Loppacher +2
    HALPreprintLicence not statedGeneral physicsHAL

Cite

BibTeXRIS
BibTeX
@article{imakawa2026highspeed,
  title = {{High-Speed Atomic Force Microscopy Reveals Single-Molecule Dynamics of Fulvestrant-Bound Estrogen Receptor α.}},
  author = {Reon Imakawa and Kota Aramaki and Takeru Kajiyama and Kota Yoshimura and Towa Onohara and Keesiang Lim and Richard W Wong and Ayami Matsushima},
  journal = {The journal of physical chemistry letters},
  year = {2026},
  month = sep,
  doi = {10.1021/acs.jpclett.6c01784},
  url = {https://europepmc.org/article/MED/42915481},
  note = {CC BY-NC-ND},
}
RIS
TY  - JOUR
TI  - High-Speed Atomic Force Microscopy Reveals Single-Molecule Dynamics of Fulvestrant-Bound Estrogen Receptor α.
AU  - Reon Imakawa
AU  - Kota Aramaki
AU  - Takeru Kajiyama
AU  - Kota Yoshimura
AU  - Towa Onohara
AU  - Keesiang Lim
AU  - Richard W Wong
AU  - Ayami Matsushima
PY  - 2026
DA  - 2026/09/01
JO  - The journal of physical chemistry letters
DO  - 10.1021/acs.jpclett.6c01784
UR  - https://europepmc.org/article/MED/42915481
AB  - Fulvestrant is a selective estrogen receptor downregulator (SERD) that antagonizes estrogen receptor α (ERα) and also promotes receptor degradation. However, how it affects full-length ERα dynamics at the single-molecule level remains unclear. Here, we used high-speed atomic force microscopy (HS-AFM) to directly visualize the dynamic behavior of full-length ERα under fulvestrant-bound, ligand-free, and other ligand-bound conditions. Among the four conditions, fulvestrant-bound ERα alone showed a reduced apparent molecular volume and increased surface mobility, behaving distinctly from the ligand-free, E2-bound, and 4-OHT-bound states. These results indicate that fulvestrant not only drives ERα inactivation and degradation but also is associated with changes in the observed molecular morphology and dynamics of full-length ERα. Our study provides direct single-molecule observation of altered molecular behavior under fulvestrant-bound conditions, which we interpret as reflecting changes in the conformational ensemble of full-length ERα.
SN  - 1948-7185
ER  -