Fields of Research
- Ion channel pharmacology
- Protein structure and function
- Molecular basis of disease
- Drug discovery and precision medicine
Research Summary
We decode the atomic architecture of ion channels to reveal how drugs, toxins, and disease mutations rewire cellular electrical signaling—and turn that knowledge into the next generation of targeted therapeutics
Research Statement
The Wisedchaisri Lab investigates the structure and mechanism of voltage-gated ion channels, their interactions with drugs and neurotoxins, and the structural basis of human channelopathies caused by disease-associated mutations. We combine structural biology approaches, including X-ray crystallography and cryogenic electron microscopy (cryo-EM), with biochemistry and electrophysiology to perform comprehensive structural and functional studies of ion channels. Our goal is to uncover fundamental mechanistic insights that advance our understanding of ion channel function in health and disease and enable the development of innovative therapeutic strategies.
Awards and Honors
In the News
Atomic-level study captures frog toxin in action
Faculty
- Building:
- Health Sciences Building
- Room:
- E-425
- Box:
- 357280
- Phone:
- 206-685-2233
Lab
- Box:
- 357280
- Phone:
- 206-685-2233
Select Publications
1. Catterall, W.A.#, Gamal El-Din, T.M.#, and Wisedchaisri,G.# (2024) The chemistry of electrical signaling in sodium channels from bacteria and beyond. Cell Chem. Biol. 31(8), 1405-21. (#Corresponding authors)
2. Tonggu, L.*, Wisedchaisri, G.*, Gamal El-Din, T.M.*, Lenaeus, M.J., Logan, M.M., Toma, T., Du Bois, J., Zheng, N., and Catterall, W.A. (2024) Dual receptor-sites reveal the structural basis for hyperactivation of sodium channels by poison-dart toxin batrachotoxin. Nature Communications, 15(1), 2306. (*Equal contribution)
3. Wisedchaisri, G.#, Gamal El-Din, T.M., Powell, N.M., Zheng, N., and Catterall, W.A. (2023) Structural Basis for Severe Pain Caused by Mutations in the Voltage Sensors of Sodium Channel NaV1.7. J. Gen. Physiol., 155(12):e202313450. (#Corresponding author)
4. Wisedchaisri, G., Gamal El-Din, T.M., Zheng, N., and Catterall, W.A. (2023) Structural Basis for Severe Pain Caused by Mutations in the S4-S5 Linkers of Voltage-Gated Sodium Channel NaV1.7. Proc. Natl. Acad. Sci. U.S.A., 120(14), e2219624120.
5. Wisedchaisri, G.# and Gamal El-Din, T.M.# (2022) Druggability of Voltage-gated Sodium Channels – Exploring Old and New Drug Receptor Sites. Front. Pharmacol. 13, 858348. (#Corresponding authors)
6. Wisedchaisri, G.*, Tonggu, L.*, Gamal El-Din, T.M., McCord, E., Zheng, N., and Catterall, W.A. (2021) Structural basis for high-affinity trapping of the NaV1.7 channel in its resting state by tarantula toxin. Molecular Cell, 81(1), 38-48.e4. (*Equal contribution)
7. Catterall, W.A., Wisedchaisri, G., Zheng, N. (2020) The conformational cycle of a prototypical voltage-gated sodium channel. Nature Chemical Biology 16(12), 1314-20.
8. Wisedchaisri, G., Tonggu, L., McCord, E., Gamal El-Din, T.M., Wang, L., Zheng, N., Catterall, W.A. (2019) Resting-state structure and gating mechanism of a voltage-gated sodium channel. Cell 178(4), 993-1003.e12.
Publications
