General anesthetic binding mode via hydration with weak affinity and molecular discrimination: General anesthetic dissolution in interfacial water of the common binding site of GABA receptor.

The GABA receptor (GABAR) is a target channel for the loss of awareness of general anesthesia. General anesthetic (GA) spans a wide range of chemical structures, such as monatomic molecules, barbital acids, phenols, ethers, and alkanes. GA has a weak binding affinity, and the affinity has a characteristic that correlates with the solubility in olive oil rather than the molecular shape.

Deuterium oxide protects against myocardial injury induced by ischemia and reperfusion in rats.

. Although deuterium oxide (DO) has preservative property on the extracted organ, whether DO also protects the in situ myocardial injury remains unknown. Using cardiac microdialysis, local administration of DO through dialysis probe was applied in situ rat heart.

Identification of Verapamil Binding Sites Within Human Kv1.5 Channel Using Mutagenesis and Docking Simulation.

Background/aims: The phenylalkylamine class of L-type Ca channel antagonist verapamil prolongs the effective refractory period (ERP) of human atrium, which appears to contribute to the efficacy of verapamil in preventing reentrant-based atrial arrhythmias including atrial fibrillation. This study was designed to investigate the molecular and electrophysiological mechanism underlying the action of verapamil on human Kv1.5 (hKv1.

Interactions of Propofol With Human Voltage-gated Kv1.5 Channel Determined by Docking Simulation and Mutagenesis Analyses.

Propofol blocks the voltage-gated human Kv1.5 (hKv1.5) channel by preferentially affecting in its open state.

Putative binding sites for arachidonic acid on the human cardiac Kv 1.5 channel.

Background And Purpose: In human heart, the Kv 1.5 channel contributes to repolarization of atrial action potentials. This study examined the electrophysiological and molecular mechanisms underlying arachidonic acid (AA)-induced inhibition of the human Kv 1.

Noble gas binding to human serum albumin using docking simulation: nonimmobilizers and anesthetics bind to different sites.

Background: Nonimmobilizers are structurally similar to anesthetics, but do not produce anesthesia at clinically relevant concentrations. Xenon, krypton, and argon are anesthetics, whereas neon and helium are nonimmobilizers. The structures of noble gases with anesthetics or nonimmobilizers are similar and their interactions are simple.

[New theories in molecular mechanisms of general anesthesia].

The controversy of the specific and non-specific theories of general anesthesia continues. Recently, non-specific theory began to have the persuasive power again. Molecular dynamics of target protein of the anesthesia and hydrophobic dehydration due to anesthetic binding to the protein have been drawing researcher's attention.

Three-dimensional distribution function theory for the prediction of protein-ligand binding sites and affinities: application to the binding of noble gases to hen egg-white lysozyme in aqueous solution.

The three-dimensional distribution function theory of molecular liquids is applied to lysozyme in mixtures of water and noble gases. The results indicate that the theory has the capability of predicting the protein-ligand binding sites and affinities. First, it is shown that the theory successfully reproduces the binding sites of xenon found by X-ray crystallography.

Anesthetic management of an extremely obese patient.

We present the case of a morbidly obese woman, with a body mass index (BMI) of 73.7 kg.m(-2), who had a gynecological operation under combined general and epidural anesthesia.

Theoretical study of volume changes accompanying xenon-lysozyme binding: implications for the molecular mechanism of pressure reversal of anesthesia.

The change in partial molar volume (PMV) accompanying the xenon-lysozyme binding was investigated for elucidating the molecular mechanism of the pressure reversal of general anesthesia, using the three-dimensional reference interaction site model theory of molecular solvation. An increase of the PMV from xenon binding to the substrate binding site of lysozyme was found, and the binding is suppressed by pressure, while the internal site binding did not change the PMV. The PMV change was analyzed by decomposing it into several contributions from geometry and hydration.