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- W2168307746 abstract "The suggestion by Robert Cantor, that drug-induced pressure changes in lipid bilayers can change the conformational equilibrium between open and closed states of membrane proteins and thereby cause anesthesia, attracted much attention lately. Here, we studied the effect of both large external pressure and of 1-alkanols of different chain lengths--some of them anesthetics, others not--on the lateral pressure profiles across dimyristoylphosphatidylcholine (DMPC) bilayers by molecular dynamics simulations. For a pure DMPC bilayer, high pressure both reduced and broadened the tension at the interface hydrophobic/hydrophilic and diminished the repulsion between the phospholipid headgroups. Whereas the effect of ethanol on the lateral pressure profile was similar to the effect of a large external pressure on a DMPC bilayer, long-chain 1-alkanols significantly amplified local maxima and minima in the lateral pressure profile. For most 1-alkanols, external pressure had moderate effects and did not reverse the changes 1-alkanols exerted on the pressure profile. Nevertheless, assuming the bent helix model as a simple geometric model for the transmembrane region of a membrane protein, protein conformational equilibria were shifted in opposite directions by addition of 1-alkanols and additional application of external pressure." @default.
- W2168307746 created "2016-06-24" @default.
- W2168307746 creator A5050790406 @default.
- W2168307746 creator A5083192211 @default.
- W2168307746 date "2008-12-01" @default.
- W2168307746 modified "2023-10-18" @default.
- W2168307746 title "The Influence of 1-Alkanols and External Pressure on the Lateral Pressure Profiles of Lipid Bilayers" @default.
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- W2168307746 doi "https://doi.org/10.1529/biophysj.108.142125" @default.
- W2168307746 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2599843" @default.
- W2168307746 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18849412" @default.
- W2168307746 hasPublicationYear "2008" @default.
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