@article {4611,
	title = {A H-1-NMR study of the permeation of glycolic acid through phospholipid membranes},
	journal = {Biochimica Et Biophysica Acta-Biomembranes},
	volume = {1416},
	number = {1-2},
	year = {1999},
	note = {ISI Document Delivery No.: 162BFTimes Cited: 10Cited Reference Count: 31},
	month = {Jan},
	pages = {333-338},
	type = {Article},
	abstract = {The transmembrane permeability coefficient of the alpha-hydroxyacid, glycolic acid, has been measured for egg phosphatidylcholine large unilamellar vesicles. The determination of the vesicle concentration independent first-order rate constant for membrane transport and the permeability coefficient were made using an NMR technique employing shift agents. Both the temperature dependence and the dependence on cholesterol content were investigated. The activation energy and the Arrhenius pre-exponential factor were found to be dependent on the cholesterol content. A marked increase in both parameters was observed up to 20 mol\% cholesterol, with a further, small increase up to 50\%. The pH dependence of permeability was also investigated. An increase in permeability is observed with a decrease in pH, providing a possible explanation for the effectiveness of glycolic acid in skin treatment. (C) 1999 Published by Elsevier Science B.V. All rights reserved.},
	keywords = {ACETIC-ACID, acne, aging of the, BILAYER-MEMBRANES, CHOLESTEROL, CHOLESTEROL CONTENT, glycolic acid, H-1-NMR, HUMAN ERYTHROCYTES, LAIDLAWII-B-CELLS, LARGE UNILAMELLAR VESICLES, lipid, NONELECTROLYTE, NUCLEAR MAGNETIC-RESONANCE, permeability, SKIN, transmembrane permeability, TRANSPORT, WATER},
	isbn = {0005-2736},
	url = {<Go to ISI>://000078324700030},
	author = {Males, R. G. and Herring, F. G.}
}
@article {4487,
	title = {Unusual electrostatic effects on binding of C1q to anionic liposomes: Role of anionic phospholipid domains and their line tension},
	journal = {Biochemistry},
	volume = {38},
	number = {25},
	year = {1999},
	note = {ISI Document Delivery No.: 211AUTimes Cited: 19Cited Reference Count: 61},
	month = {Jun},
	pages = {8112-8123},
	type = {Article},
	abstract = {The binding of I-125-C1q to anionic liposomes was studied as a function of protein concentration, pH, ionic strength, and anionic lipid composition. The maximum amount of protein bound per micromole of lipid was very sensitive to electrostatic factors, increasing strongly with decreased pH and ionic strength or increased anionic Lipid content. The apparent association constant was independent of these electrostatic factors, however, in marked contrast to studies on basic peptide binding Co anionic lipid vesicles. Microscopic observations of large unilamellar Liposomes containing fluorescently labeled C1q or phosphatidylglycerol demonstrated, under conditions causing strong electrostatic interactions, that C1q and anionic lipids colocalized into domains whose radii of curvature were higher than that of the surrounding lipid. These domains were observed to bud and pinch off into brightly fluorescent vesicles. We propose a model for all of these observations in which the line tension or edge energy at the boundary of the domain resists its increase in circumference as the domain grows by electrostatic effects on binding, eventually resulting in vesiculation. We propose that under favorable electrostatic conditions, as larger domains form the edge energy balances the increases in the electrostatic contribution to binding, resulting in a net binding energy independent of electrostatic factors.},
	keywords = {5-BISPHOSPHATE, ACIDIC LIPIDS, ACTIVATES, BASIC PEPTIDES, COMPLEMENT, COMPLEMENT SUBCOMPONENT C1Q, HEPATIC-UPTAKE, LARGE UNILAMELLAR VESICLES, LATERAL DOMAINS, MEMBRANE DOMAINS, PHOSPHATIDYLINOSITOL 4, PROTEIN-KINASE-C},
	isbn = {0006-2960},
	url = {<Go to ISI>://000081138400028},
	author = {Bradley, A. J. and Maurer-Spurej, E. and Brooks, D. E. and Devine, D. V.}
}
@article {4346,
	title = {Equations describing passive transport through vesicular membranes},
	journal = {Biophysical Chemistry},
	volume = {70},
	number = {1},
	year = {1998},
	note = {ISI Document Delivery No.: YU539Times Cited: 4Cited Reference Count: 26},
	month = {Jan},
	pages = {65-74},
	type = {Article},
	abstract = {A theoretical description of the kinetics of the passive transport of both lipophobic and lipophilic nonelectrolytes, weak acids, and weak bases through membranes of large unilamellar vesicles is discussed. Equations are derived which may be used to obtain permeability coefficients and predict the extent of LW entrapment of permeant molecules. Theoretical curves are generated to illustrate the difference between lipophobic and lipophilic permeation. By applying a diffusional approach rather than a simple first order kinetic approach to the problem of passive transport, some of the inconsistencies observed in other works are corrected. (C) 1998 Elsevier Science B.V.},
	keywords = {accumulation, DIFFUSION, FATTY-ACIDS, IONS, KINETICS, LARGE UNILAMELLAR VESICLES, lipid bilayer, LIPID BILAYER-MEMBRANES, LIPOSOMES, PARTITION-COEFFICIENTS, passive, permeability, PROCEDURE, RAPID EXTRUSION, TRANSMEMBRANE PH GRADIENTS, TRANSPORT},
	isbn = {0301-4622},
	url = {<Go to ISI>://000071728000007},
	author = {Males, R. G. and Phillips, P. S. and Herring, F. G.}
}
@article {4210,
	title = {Inhibition of liposome-induced complement activation by incorporated poly(ethylene glycol) lipids},
	journal = {Archives of Biochemistry and Biophysics},
	volume = {357},
	number = {2},
	year = {1998},
	note = {ISI Document Delivery No.: 119UCTimes Cited: 65Cited Reference Count: 50},
	month = {Sep},
	pages = {185-194},
	type = {Article},
	abstract = {Complement activation causes opsonization of foreign particles leading to particle elimination from the blood. Complement-mediated opsonization of charged and large liposomes presents a fundamental problem in their use to deliver therapeutic agents in vivo. To prolong the circulation half-lives of such liposomes, complement activation must be curtailed. The aim of this study was to assess the ability of poly(ethylene glycol)-lipids (PEG-lipids) to inhibit the in vitro activation of the classical pathway of complement in human serum by anionic liposomes. Incorporation of cholesterol-PEG(600) (CH-PEG(600)), cholesterol-PEG(1000) (CH-PEG(1000)), or phosphatidylethanolamine-PEG(2000) (PE-PEG(2000)) resulted in dose-dependent inhibition of Clq binding and complement activation. The dose of PEG-lipid at which complement activation was blocked was inversely related to the PEG chain length. Complement activation was strongly inhibited when 15 mole\% of CH-PEG(600), 10 mole\% CH-PEG(1000), or 5 mole\% PE-PEG(2000), was incorporated into 100-nm anionic liposomes. PEG-lipid incorporation into larger liposomes (240 nm) was also successful in blocking C1q binding and complement activation. Radiolabeled cholesterol-PEG(similar to 1400) was prepared and used to determine both the percentage of CH-PEG incorporated into the liposomes and the percentage maintained in the liposomes in the presence of 50\% human serum at 37 degrees C for up to 24 h. (C) 1998 Academic Press.},
	keywords = {C1q, CHOLESTEROL, CLEARANCE, complement activation, HEPATIC-UPTAKE, INVIVO, LARGE UNILAMELLAR VESICLES, LIPOSOMES, POLY(ETHYLENE GLYCOL), POLYETHYLENE-GLYCOL, PROLONGED CIRCULATION TIME, SERUM, SIZE, SURFACE-CHARGE},
	isbn = {0003-9861},
	url = {<Go to ISI>://000075915200002},
	author = {Bradley, A. J. and Devine, D. V. and Ansell, S. M. and Janzen, J. and Brooks, D. E.}
}
