Partitioning of a Fluorescent Phospholipid Between Fluid Bilayers: Dependence on Host Lipid Acyl Chains

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 1997 Dec 31

PMID 9414223

Citations 4

Authors

G W Feigenson

Affiliations

Soon will be listed here.

Abstract

The partition coefficient Kp was measured for a headgroup-labeled phospholipid (12:0,12:0)-N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-PE (12-NBD-PE), equilibrated between LUV of a series of phosphatidylcholines (PC). Fluorescence resonance energy transfer between the 12-NBD-PE and a headgroup-rhodamine-labeled PE was used to find the equilibrium concentration of the 12-NBD-PE in the different LUV. Reliable equilibrium concentrations were obtained by monitoring the approach to equilibrium starting from a concentration below and from a concentration above the ultimate values. Using (16:0,18:1delta9)-PC as the reference lipid, Kp ranged from a high value of 1.65 favoring (16:0,18:1delta9)-PC over (16:1delta9,16:1delta9)-PC, to a low value of 0.90, favoring (22:1delta13,22:1delta13)-PC over (16:0,18:1delta9)-PC. The Kp values enabled calculation of the acyl chain contribution to the excess free energy of mixing for (12:0,12:0) acyl chains at infinite dilution in the L alpha phase of PC having acyl chains of (16:0,18:1delta9), (16:1delta9,16:1delta9), (18:1delta9,18:1delta9), (18:1delta6,18:1delta6), (20:1delta11,20:1delta11), and (22:1delta13,22:1delta13). (14:1delta9,14:1delta9)-PC was found to transfer so rapidly between LUV as to preclude reliable Kp measurement.

Citing Articles

Calibration of Distribution Analysis of the Depth of Membrane Penetration Using Simulations and Depth-Dependent Fluorescence Quenching.

Kyrychenko A, Rodnin M, Ladokhin A J Membr Biol. 2014; 248(3):583-94.

PMID: 25107303 PMC: 4321973. DOI: 10.1007/s00232-014-9709-1.

Kinetics and thermodynamics of association of a phospholipid derivative with lipid bilayers in liquid-disordered and liquid-ordered phases.

Abreu M, Moreno M, Vaz W Biophys J. 2004; 87(1):353-65.

PMID: 15240470 PMC: 1304356. DOI: 10.1529/biophysj.104.040576.

Binding of a fluorescent lipid amphiphile to albumin and its transfer to lipid bilayer membranes.

Abreu M, Estronca L, Moreno M, Vaz W Biophys J. 2003; 84(1):386-99.

PMID: 12524292 PMC: 1302620. DOI: 10.1016/S0006-3495(03)74859-0.

Partitioning of amphiphiles between coexisting ordered and disordered phases in two-phase lipid bilayer membranes.

Mesquita R, Melo E, Thompson T, Vaz W Biophys J. 2000; 78(6):3019-25.

PMID: 10827980 PMC: 1300885. DOI: 10.1016/S0006-3495(00)76840-8.

References

Silvius J, Leventis R . Spontaneous interbilayer transfer of phospholipids: dependence on acyl chain composition. Biochemistry. 1993; 32(48):13318-26. DOI: 10.1021/bi00211a045. View

Wimley W, Thompson T . Transbilayer and interbilayer phospholipid exchange in dimyristoylphosphatidylcholine/dimyristoylphosphatidylethanolamine large unilamellar vesicles. Biochemistry. 1991; 30(6):1702-9. DOI: 10.1021/bi00220a036. View

Gruber H, Schindler H . External surface and lamellarity of lipid vesicles: a practice-oriented set of assay methods. Biochim Biophys Acta. 1994; 1189(2):212-24. DOI: 10.1016/0005-2736(94)90068-x. View

Nichols J, Pagano R . Use of resonance energy transfer to study the kinetics of amphiphile transfer between vesicles. Biochemistry. 1982; 21(8):1720-6. DOI: 10.1021/bi00537a003. View

Shahinian S, Silvius J . Doubly-lipid-modified protein sequence motifs exhibit long-lived anchorage to lipid bilayer membranes. Biochemistry. 1995; 34(11):3813-22. DOI: 10.1021/bi00011a039. View

Shin T, Leventis R, Silvius J . Partitioning of fluorescent phospholipid probes between different bilayer environments. Estimation of the free energy of interlipid hydrogen bonding. Biochemistry. 1991; 30(30):7491-7. DOI: 10.1021/bi00244a018. View

Lin H, Li S, Wang G, Brumbaugh E, Huang C . A calorimetric study of binary mixtures of saturated and monounsaturated mixed-chain phosphatidylethanolamines. Biochim Biophys Acta. 1996; 1283(2):199-206. DOI: 10.1016/0005-2736(96)00093-4. View

Roseman M, Thompson T . Mechanism of the spontaneous transfer of phospholipids between bilayers. Biochemistry. 1980; 19(3):439-44. DOI: 10.1021/bi00544a006. View

Pownall H, Bick D, Massey J . Spontaneous phospholipid transfer: development of a quantitative model. Biochemistry. 1991; 30(23):5696-700. DOI: 10.1021/bi00237a009. View

10.

Caffrey M, Feigenson G . Fluorescence quenching in model membranes. 3. Relationship between calcium adenosinetriphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics. Biochemistry. 1981; 20(7):1949-61. DOI: 10.1021/bi00510a034. View

11.

Nibu Y, Inoue T, Motoda I . Effect of headgroup type on the miscibility of homologous phospholipids with different acyl chain lengths in hydrated bilayer. Biophys Chem. 1995; 56(3):273-80. DOI: 10.1016/0301-4622(95)00041-u. View

12.

Nichols J, Pagano R . Kinetics of soluble lipid monomer diffusion between vesicles. Biochemistry. 1981; 20(10):2783-9. DOI: 10.1021/bi00513a012. View