The binding of ethanol-d6 to dipalmityl-phosphatidylcholine liposomes (DPPC) can be separated into two processes, namely, ethanol in the bilayer and on the surface of the bilayer. For the deuterons of the methylene group, the T2 of both bound states is shorter than the respective preexchange lifetime (τB) and therefore the amount of ethanol bound to both sites can be determined from the decrease in the methylene intensity resonance in the presence of DPPC. For the methyl resonance, however, only the T2 of deuterons on ethanol bound to the surface is less than its τB and the amount of surface bound ethanol-d6 can be determined. Subtraction yields the amount of ethanol bound within the bilayer. The partion coefficient for internally bound ethanol remains constant from 0 to 3.5 m ethanol. Surface binding is, however, highly cooperative.
|Original language||English (US)|
|Number of pages||5|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Jul 16 1985|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology