The interaction of phenol with lipid bilayers.
The depression of the phase-transition temperature of dimyristoyl- and dipalmitoylphosphatidylcholine vesicles induced by phenol has been investigated by fluorescence polarization. This effect is strongly pH and concentration dependent. Only the uncharged phenol molecule influences the fluidity of the bilayer so that the interaction of phenol with the bilayer can be situated in the hydrophobic acyl chain region. Direct measurements of the partitioning of phenol in the phospholipid vesicles confirm these results and show a limited and concentration-dependent solubility. Phase-transition temperature depressions, obtained from thermodynamic analysis of partition coefficient measurement, are in good agreement with the experimental values.
D004134:Dimyristoylphosphatidylcholine / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008051:Lipid Bilayers / Q000378:metabolism*; D008081:Liposomes / Q000378:metabolism; D008560:Membrane Fluidity; D019800:Phenol; D010636:Phenols / Q000378:metabolism*; D011663:Pulmonary Surfactants / Q000378:metabolism*; D013696:Temperature; D013816:Thermodynamics
D008051:Lipid Bilayers; D008081:Liposomes; D010636:Phenols; D011663:Pulmonary Surfactants; D019800:Phenol; D004134:Dimyristoylphosphatidylcholine