Journal of Molecular Biology
CommunicationThe Specific Binding Site of the Volatile Anesthetic Diiodomethane to Purple Membrane by X-ray Diffraction
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Cited by (21)
Interaction of anesthetic molecules with α-helix and polyproline II extended helix of long-chain poly-L-lysine
2018, Spectrochimica Acta - Part A: Molecular and Biomolecular SpectroscopyCitation Excerpt :Little is known about the structural features of potential molecular targets of anesthetics. It is accepted that anesthetic binding sites exist on both protein and lipid molecules [1–6]. In the case of lipid-anesthetic systems, a nonspecific interaction dominates, while protein proponents favor a specific interaction.
Effect of Xenon Binding to a Hydrophobic Cavity on the Proton Pumping Cycle in Bacteriorhodopsin
2008, Journal of Molecular BiologyPrediction of volatile anesthetic binding sites in proteins
2006, Biophysical JournalCitation Excerpt :VAs interact with many cellular components, yet anesthetic effects ultimately manifest as changes in protein function. VAs have been shown to accumulate at the aqueous interface of a dipalmitoylphosphatidylcholine membrane (1) and at the protein-lipid interface region near the surface of purple membrane (2). VAs are known to bind to transmembrane proteins such as the plasma membrane Ca2+-ATPase (3), rhodopsin (4), the nicotinic acetylcholine receptor (5,6), and several proteins from rat neuronal membranes, assayed in vitro (7).
Effects of normal alcohols and isoflurane on lipid headgroup dynamics in nicotinic acetylcholine receptor-rich lipid vesicles
2000, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :Even in the context of our findings, it is still possible that lipid membranes contribute to anesthetic actions at receptors. For example, an investigation of X-ray structure and function of membrane protein with the volatile anesthetic analogue, bacteriorhodopsin with diiodomethane, demonstrated that diiodomethane binds to the interfacial sites between protein and lipid and reduces the longevity of M-intermediate in flash photolysis [29]. As a further example, sodium channels were reconstituted into membranes in which lipid composition was systemically altered by the addition of cholesterol.
The quantitative analysis of three action modes of volatile anesthetics on purple membrane
2000, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :Thus, we can consider the possibility that the same action as mode I in PM occurs generally in anesthesia. We have previously reported that, in mode I, anesthetic molecules bind to the protein–lipid interface near the surface of PM based on X-ray diffraction experiments with heavy atoms containing the anesthetic molecule diiodomethane [7]. TI also contains a heavy iodine atom, and X-ray diffraction experiments show the same binding position as that found in diiodomethane [12].
The uncoupling of bacteriorhodopsin by high temperature and anaesthetics
1998, Toxicology Letters