| Autor: |
Dubey AK; Department of Pathology, Anatomy and Cell Biology, Medical College of Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA., Eryomin VA, Taraschi TF, Janes N |
| Jazyk: |
angličtina |
| Zdroj: |
Biophysical journal [Biophys J] 1996 May; Vol. 70 (5), pp. 2307-15. |
| DOI: |
10.1016/S0006-3495(96)79796-5 |
| Abstrakt: |
Implicit within the concept of membrane-buffer partition coefficients of solutes is a nonspecific solvation mechanism of solute binding. However, (2)H NMR studies of the binding of (2)H(6)-ethanol and [1-(2)H(2)] n-hexanol to phosphatidylcholine vesicles have been interpreted as evidence for two distinct alcohol binding modes. One binding mode was reported to be at the membrane surface. The second mode was reported to be within the bilayer interior. An examination of the (2)H NMR binding studies, together with direct radiolabel binding assays, shows that other interpretations of the data are more plausible. The results are entirely consistent with partitioning (nonspecific binding) as the sole mode of alcohol binding to liposomes, in accord with our previous thermodynamic interpretation of alcohol action in phosphatidylcholine liposomes. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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