Lipid bilayers determine allostery but not intrinsic affinity of cAMP to pacemaker channels
Vinay Idikuda, Susovan Roy Chowdhury, Audrey Chinn, Yongchang Chang, Suhaila Rahman, Qian Ren, Huan Bao, Ziao Fu, Randall H. Goldsmith, Baron Chanda · 2026
Read Lipid bilayers determine allostery but not intrinsic affinity of cAMP to pacemaker channels by Vinay Idikuda, Susovan Roy Chowdhury, Audrey Chinn, Yongchang Chang, Suhaila Rahman, Qian Ren, Huan Bao, Ziao Fu, Randall H. Goldsmith, Baron Chanda (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13332177.txt.
Description
Vinay Idikuda and nine co-authors study how cAMP binds to pacemaker channels, in work published in 2026. These HCN channels help set heart rhythm, and cAMP binding controls their activity. The team placed purified human channels into lipid nanodiscs and measured binding step by step with nanophotonic waveguides.
In lipid bilayers, cAMP molecules bound cooperatively, unlike channels held in detergents. The first molecule's affinity stayed the same across settings, so the bilayer changed later binding steps, not the first. Cryo-EM images showed extra lipid densities near the channels. The authors conclude that the lipid bilayer itself is enough to create cooperative binding and sharpen channel response.
Catalog record
| CREATOR | Vinay Idikuda, Susovan Roy Chowdhury, Audrey Chinn, Yongchang Chang, Suhaila Rahman, Qian Ren, Huan Bao, Ziao Fu, Randall H. Goldsmith, Baron Chanda |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 73 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |