NDLI: Structural consequences of anesthetic and nonimmobilizer interaction with gramicidin A channels.

Content Provider	PubMed Central
Author	Tang, P. Xu, Y. Simplaceanu, V.
Abstract	Although interactions of general anesthetics with soluble proteins have been studied, the specific interactions with membrane bound-proteins that characterize general anesthesia are largely unknown. The structural modulations of anesthetic interactions with synaptic ion channels have not been elucidated. Using gramicidin A as a simplified model for transmembrane ion channels, we have recently demonstrated that a pair of structurally similar volatile anesthetic and nonimmobilizer, 1-chloro-1,2,2-trifluorocyclobutane (F3) and 1,2-dichlorohexafluorocyclobutane (F6), respectively, have distinctly different effects on the channel function. Using high-resolution NMR structural analysis, we show here that neither F3 nor F6 at pharmacologically relevant concentrations can significantly affect the secondary structure of the gramicidin A channel. Although both the anesthetic F3 and the nonimmobilizer F6 can perturb residues at the middle section of the channel deep inside the hydrophobic region in the sodium dodecyl sulfate micelles, only F3, but not F6, can significantly alter the chemical shifts of the tryptophan indole N-H protons near the channel entrances. The results are consistent with the notion that anesthetics cause functional change of the channel by interacting with the amphipathic domains at the peptide-lipid-water interface.
Related Links	http://dx.doi.org/10.1016/s0006-3495(99)77391-1
Ending Page	2350
Page Count	5
Starting Page	2346
File Format	PDF
ISSN	00063495
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	5
Volume Number	76
Language	English
Publisher Date	1999-05-01
Access Restriction	Open
Subject Keyword	Biophysics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

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Distinctly different interactions of anesthetic and nonimmobilizer with transmembrane channel peptides.

General anesthetic binding to gramicidin A: the structural requirements.

Asymmetric gramicidin channels: heterodimeric channels with a single F6Val1 residue.

Effects of volatile anesthetic on channel structure of gramicidin A.

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Structural consequences of anesthetic and nonimmobilizer interaction with gramicidin A channels.

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