Interactions of saturated diacylglycerols with phosphatidylcholine bilayers: A sup 2 H NMR study
- Univ. of California, Riverside (United States)
The interactions of a series of saturated diacylglycerols (DAGs) with fatty acid side chain lengths of 6-14 carbons with multilamellar phospholipid bilayers consisting either of dipalmitoylphosphatidylcholine (DPPC) or of a mixture of DPPC and bovine liver phosphatidylcholine (BL-PC) extracts were studied by {sup 2}H NMR spectrometry. The authors found that the perturbation induced by the DAGs into the bilayer structure strongly depends on the length of the DAG fatty acid side chain. Shorter chain 1,2-sn-dihexanoylglycerol and, to a larger degree, 1,2-sn-dioctanoylglycerol (diC{sub 8}) induce transverse perturbation of the bilayer structure: the order parameters of the phospholipid side chains are increased by the intercalating DAG molecules in the region adjacent to the phospholipid headgroups and decreased toward the terminal methyls, corresponding to the bilayer interior. Each of the DAGs studied induces a decrease in the area per phospholipid molecule, and a corresponding increase in the lateral surface pressure of the bilayers. Since numerous biochemical studies consistently report that diC{sub 8} is the most effective of saturated DAGs in activating protein kinase C, they may conclude that the activation of this enzyme is associated with a transverse perturbation of the lipid bilayer structure and a decreased ordering in the interior of the bilayer membrane, and is less affected by the lateral phase separation of the lipids into regions of different fluidities, as induced by the longer chain DAGs.
- OSTI ID:
- 5687987
- Journal Information:
- Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 31:2; ISSN 0006-2960; ISSN BICHA
- Country of Publication:
- United States
- Language:
- English
Similar Records
Lysophosphatidylcholine metabolism to 1,2-diacylglycerol in lymphoblasts: Involvement of a phosphatidylcholine-hydrolyzing phospholipase C
The effect of membrane fluidization on protein kinase C: Inhibition by ethanol and higher alcohols and stimulation by increased lipid unsaturation or addition non-esterified fatty acids
Related Subjects
59 BASIC BIOLOGICAL SCIENCES
ALCOHOLS
ENZYMES
ESTERS
GLYCEROL
HYDROXY COMPOUNDS
LIPIDS
MAGNETIC RESONANCE
MEMBRANES
MOLECULAR STRUCTURE
NMR SPECTRA
NUCLEAR MAGNETIC RESONANCE
ORGANIC COMPOUNDS
ORGANIC PHOSPHORUS COMPOUNDS
PHASE STUDIES
PHOSPHOLIPIDS
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHOTRANSFERASES
PROTEINS
RESONANCE
SPECTRA
TRANSFERASES