Abstract:
:The permeability of an N-oleoyldihydrosphingomyelin bilayer against glycerol was similar to that of a bilayer of phosphatidylcholine with identical effective hydrophobic chain length. Cholesterol at 1:1 molar ratio reduced the permeability, and also reduced the energy of activation of glycerol penetration, an effect not found for diesterphosphatidylcholine with cholesterol. The higher level of the ground state of the entropy of activation for permeability can be interpreted in terms of a hydrogen belt model which postulates lipid-lipid hydrogen bonding in membranes and explains the effect found as a disturbance of the hydrogen belt structure. Dihydrosphingomyelin can be considered to function as an "extender" in the hydrogen belt network.
journal_name
Lipidsjournal_title
Lipidsauthors
Tirri LJ,Ayengar NK,Lipton LC,Chatterjie N,Brockerhoff Hdoi
10.1007/BF02533668subject
Has Abstractpub_date
1978-04-01 00:00:00pages
267-9issue
4eissn
0024-4201issn
1558-9307journal_volume
13pub_type
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