Temperature-Dependent Partitioning of Coumarin 152 in Phosphatidylcholine Lipid Bilayers
| Autor: | Heather S. Blanchard, Robert A. Walker, Christine A. Gobrogge |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
1 2-Dipalmitoylphosphatidylcholine Entropy Lipid Bilayers Analytical chemistry 010402 general chemistry 01 natural sciences Endothermic process Permeability Phase Transition Diffusion 03 medical and health sciences chemistry.chemical_compound Coumarins Phosphatidylcholine Phase (matter) Materials Chemistry Membrane fluidity Physical and Theoretical Chemistry Lipid bilayer Unilamellar Liposomes Fluorescent Dyes Chromatography Vesicle Temperature Fluorescence 0104 chemical sciences Surfaces Coatings and Films 030104 developmental biology Membrane chemistry Phosphatidylcholines Dimyristoylphosphatidylcholine Hydrophobic and Hydrophilic Interactions |
| Zdroj: | The journal of physical chemistry. B. 121(16) |
| ISSN: | 1520-5207 |
| Popis: | Partitioning of coumarin 152 (C152) in phosphatidylcholine vesicles was quantified using time-resolved fluorescence emission. Phospholipid vesicles were comprised of 1,2-dilauroyl-sn-glycero-3-phosphocholine (12:0 DLPC), 1,2-dimyristoyl-sn-glycero-3-phosphocholine (14:0 DMPC), and 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (16:0 DPPC). C152 fluorescence emission decays were fit to three lifetimes, corresponding to C152 solvated by the aqueous buffer, embedded in polar lipid headgroups, and surrounded by the nonpolar lipid membrane core. Partitioning was measured as a function of sample temperature and vesicle composition. C152 in all three lipid systems showed qualitatively similar partitioning behavior. Partitioning into a gel phase membrane was thermoneutral and slightly entropically favored. Partitioning of C152 near the lipid membrane headgroups was entropically driven and endothermic. Well above the melting temperature, exsolvation of C152 from the membrane back into the aqueous buffer was enthalpically driven but entropically unfavorable. Regardless of solution temperature, relatively little (15%) C152 partitions into the hydrophobic core of the membrane. The magnitudes of the forces driving C152 partitioning systematically increased with alkyl chain length (DLPCDMPCDPPC). Differences in partitioning between the three vesicle systems are attributed to differences in surface area per lipid as membrane phase changes from the gel to liquid-crystalline state. |
| Databáze: | OpenAIRE |
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