@article {5219,
	title = {Binding of small alcohols to a lipid bilayer membrane: does the partitioning coefficient express the net affinity?},
	journal = {Biophysical Chemistry},
	volume = {89},
	number = {1},
	year = {2001},
	note = {ISI Document Delivery No.: 397WQTimes Cited: 13Cited Reference Count: 55},
	month = {Jan},
	pages = {53-63},
	type = {Article},
	abstract = {The total vapor pressures at 26 degreesC of binary (water-alcohol) and ternary (water-alcohol-vesicle) systems were measured for sis short chain alcohols. The vesicles were unilamellar dipalmitoyl phosphatidylcholine (DMPC). The data was used to evaluate the effect of vesicles on the chemical potential of alcohols expressed as the preferential binding parameter of the alcohol-lipid interaction, Gamma (23). This quantity is a thermodynamic (model-free) measure of the net strength of membrane-alcohol interactions. For the smaller investigated alcohols (methanol, ethanol and 1-propanol) Gamma (23) was negative. This is indicative of so-called preferential hydration, a condition where the affinity of the membrane for water is higher than the affinity for the alcohol. For the longer alcohols (1-butanol, 1-pentanol, 1-hexanol) Gamma (23) was positive and increasing with increasing chain length. This demonstrates preferential binding, i.e. enrichment of alcohol in the membrane and a concomitant depletion of the solute in the aqueous bulk. The measured values of Gamma (23) were compared to the number of alcohol-membrane contacts specified by partitioning coefficients from the literature. It was found that for the small alcohols the number of alcohol-membrane contacts is much larger than the number of preferentially bound solutes. This discrepancy, which is theoretically expected in cases of very weak binding, becomes less pronounced with increasing alcohol chain length, and when the partitioning coefficient exceeds approximately 3 on the molal scale (10(2) in mole fraction units) it vanishes. Based on this, relationships between structural and thermodynamic interpretations of membrana partitioning are discussed. (C) 2001 Elsevier Science B.V. All rights reserved.},
	keywords = {energy of interaction, ETHANOL, free, lipid membranes, membrane partitioning, MODEL, NONELECTROLYTE PARTITION, PHASE, PHOSPHATIDYLCHOLINE, preferential binding, protein stability, SOLUTES, THERMODYNAMICS, vapor pressure, VAPOR-PRESSURE, WATER},
	isbn = {0301-4622},
	url = {<Go to ISI>://000166721200005},
	author = {Westh, P. and Trandum, C. and Koga,Yoshikata}
}
@article {3938,
	title = {The effect of organotin compounds on the permeability of model biological membranes},
	journal = {Applied Organometallic Chemistry},
	volume = {11},
	number = {5},
	year = {1997},
	note = {ISI Document Delivery No.: WZ733Times Cited: 7Cited Reference Count: 28Pacifichem 95 Meeting on Safety and Environmental Effects of Organometallics1995HONOLULU, HI},
	month = {May},
	pages = {369-379},
	type = {Proceedings Paper},
	abstract = {The efflux of dimethylarsinic acid (DMA) from liposomes formed from egg phosphatidylcholine (EPC) is increased when tributyltin chloride (TBT) is added to the extraliposomal compartment; however the addition of monobutyltin trichloride (MBT) slows down the efflux. When the liposomes are prepared from EPC and organotin compounds, different mechanisms for DMA efflux seem to operate: TBT-EPC liposomes show a mixture of facilitated and passive diffusion; MBT-EPC liposomes show only passive diffusion. The facilitated diffusion of DMA(-) seems to be stopped by the addition of TBT to the extraliposomal compartment. (C) 1997 by John Wiley \& Sons, Ltd.},
	keywords = {bilayer, DIMETHYLARSINIC ACID, efflux, egg, ERYTHROCYTE, EXCHANGE, facilitated diffusion, LIPOSOMES, membrane modification, monobutyltin, NMR, PHOSPHATIDYLCHOLINE, tributyltin chloride, trichloride},
	isbn = {0268-2605},
	url = {<Go to ISI>://A1997WZ73300003},
	author = {Cullen, W. R. and Herring, F. G. and Nwata, B. U.}
}
