400 MHz two-dimensional nuclear Overhauser spectroscopy on anesthetic interaction with lipid bilayer

Yokono, Satoshi; Ogli, Kenji; Miura, Shigetoshi; Ueda, I.

doi:10.1016/0005-2736(89)90068-0

Cited by 43 publications

(19 citation statements)

References 3 publications

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“…membrane) [56]. This suggestion is supported by NMR and gas chromatography studies of clinical anesthetics with macromolecular surfaces [57]. According to this view, a sufficient concentration of anesthetic compounds in the interfacial region is a prerequisite for anesthetic activity.…”

Section: Discussionmentioning

confidence: 91%

Alzheimer’s Disease: Halothane Induces Aβ Peptide to Oligomeric Form—Solution NMR Studies

et al. 2006

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Alzheimer's disease (AD) is a significant contributor to cognitive decline and is responsible for about half of the cases of dementia in later life. Although exact etiology of AD is not known, however, many risk factors for AD are identified. Anesthesia for elderly patients is considered as a risk factor in AD as they frequently experience deterioration in cognitive function with long exposure to anesthetics during surgery. Inhaled anesthetic agents remain the mainstay for patients undergoing major surgical operations. This study using multidimensional NMR spectroscopy provides the first direct evidence in vitro that inhaled anesthetic, halothane specifically interacts with Abeta40 and Abeta42 peptide. Halothane induces structural alternation of Abeta peptide from soluble monomeric alpha-helical form to oligomeric beta-sheet conformation, which may hasten the onset of AD. Abeta42 is more prone to oligomerization compared to Abeta40 in the presence of halothane. The molecular mechanism of halothane induced structural alternation of Abeta peptide is discussed.

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Section: Discussionmentioning

confidence: 91%

Alzheimer’s Disease: Halothane Induces Aβ Peptide to Oligomeric Form—Solution NMR Studies

et al. 2006

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“…It has been suggested that anesthesia might result from molecular interactions at the interface between aqueous and nonpolar media (e.g., membrane) (30). This suggestion is supported by NMR and gas chromatography studies of clinical anesthetics with macromolecular surfaces (31). Recent progress in computational studies of membrane-aqueous interfaces has made it possible to determine concentration profiles of anesthetics across these interfaces by computer simulations (32).…”

Section: Resultsmentioning

confidence: 99%

Molecular Understanding of Αβ Peptide Interaction with Isoflurane, Propofol, and Thiopental: NMR Spectroscopic Study

2006

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Abeta peptide is the major component of senile plaques (SP), which accumulate in the brain of a patient with Alzheimer's disease (AD). A recent report indicated that isoflurane enhanced Abeta oligomerization (micro-aggregation) and subsequent cytotoxicity of the Abeta peptide. A separate study showed that a clinically relevant concentration of isoflurane induces apoptosis and increases Abeta production in a human neuroglioma cell line. In vitro studies have indicated that halothane interacts specifically with Abeta peptide to induce oligomerization and that Abeta42 oligomerizes faster than Abeta40. The specific interactions of isoflurane, propofol, and thiopental with uniformly 15N labeled Abeta40 and Abeta42 peptide were investigated using multidimensional nuclear magnetic resonance (NMR) experiments. We found that isoflurane and propofol (at higher concentration) interact with Abeta40 peptides and induce Abeta oligomerization. Thiopental does not interact with specific residues (G29, A30, and I31) of Abeta40; hence, the peptide remains in the monomeric form. On the basis of our NMR study, thiopental does not oligomerize Abeta40 even at higher concentrations.

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“…This is the first description of the STD technique used to screen proteins for anesthetic binding, although various other NMR methods have been used to study anestheticprotein interactions. The interactions of anesthetics with lipids, peptides, and proteins have been studied with 19 F NMR (Dubois and Evers, 1992;Xu et al, 2000) and selective homonuclear NOE (Yokono et al, 1989;Tang et al, 1999) and heteronuclear NOE (Xu and Tang, 1997) methods. Selective saturation is only possible in molecules with preassigned resonances, a task that is prohibitive for protein screening and impossible for proteins much over 25 kDa.…”

Section: Discussionmentioning

confidence: 99%

Saturation Transfer Difference Nuclear Magnetic Resonance Spectroscopy As a Method for Screening Proteins for Anesthetic Binding

Streiff¹,

Juranić

Macura³

et al. 2004

Mol Pharmacol

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The effects of anesthetics on cellular function may result from direct interactions between anesthetic molecules and proteins. These interactions have a low affinity and are difficult to characterize. To identify proteins that bind anesthetics, we used nuclear magnetic resonance saturation transfer difference (STD) spectroscopy. The method is based on the nuclear Overhauser effect between bound anesthetic protons and all protein protons. To establish STD as a method for testing anesthetic binding to proteins, we conducted measurements on a series of protein/anesthetic solutions studied before by other methods. STD was able to identify

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400 MHz two-dimensional nuclear Overhauser spectroscopy on anesthetic interaction with lipid bilayer

Cited by 43 publications

References 3 publications

Alzheimer’s Disease: Halothane Induces Aβ Peptide to Oligomeric Form—Solution NMR Studies

Alzheimer’s Disease: Halothane Induces Aβ Peptide to Oligomeric Form—Solution NMR Studies

Molecular Understanding of Αβ Peptide Interaction with Isoflurane, Propofol, and Thiopental: NMR Spectroscopic Study

Saturation Transfer Difference Nuclear Magnetic Resonance Spectroscopy As a Method for Screening Proteins for Anesthetic Binding

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