Substituted cysteine modification and protection indicates selective interactions of the anesthetic photolabel pTFD-di-iPr-BnOH with α+/β– and α+/γ– transmembrane subunit interfaces of synaptic GABAA receptors

SCAMP results further support the hypothesis that pTFD-di-iPr-BnOH binds selectively in α+/β- and α+/γ- interfacial sites that are homologs of the β+/α- etomidate sites.

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Publication Details

Journal
PLoS ONE
Published
2025-11-06
DOI
https://doi.org/10.1371/journal.pone.0336606
Primary Topic
Photochromic and Fluorescence Chemistry
Type
article
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article

Substituted cysteine modification and protection indicates selective interactions of the anesthetic photolabel pTFD-di-iPr-BnOH with α+/β– and α+/γ– transmembrane subunit interfaces of synaptic GABAA receptors

Stuart A. Forman, Kieran Bhave
PLoS ONE
Photochromic and Fluorescence Chemistry
article

Substituted cysteine modification and protection indicates selective interactions of the anesthetic photolabel pTFD-di-iPr-BnOH with α+/β– and α+/γ– transmembrane subunit interfaces of synaptic GABAA receptors

Stuart A. Forman, Kieran Bhave
article en

Abstract

SCAMP results further support the hypothesis that pTFD-di-iPr-BnOH binds selectively in α+/β- and α+/γ- interfacial sites that are homologs of the β+/α- etomidate sites.

PLoS ONEVol. 20(11)
Massachusetts General Hospital (US)
Openalex Percentile: Top 74%
Photochromic and Fluorescence Chemistry
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