Disease relevance of Dimyristoylphosphatidylglycerol

• The outer membrane protein OmpA and the ferrichrome-iron receptor FhuA from the outer membrane of Escherichia coli were reconstituted in bilayers of dimyristoylphosphatidylglycerol [1].
• The gel-to-crystalline phase transition of DMPG shifts to higher temperatures with a concomitant dehydration of the interfacial region [2].
• At this concentration, H. salinarum archaeosomes and DMPC/DMPG/CHOL ester liposomes caused about 2% and 4% hemolysis, respectively [3].

High impact information on Dimyristoylphosphatidylglycerol

• The pharmacokinetics, organ distribution, and 24-hr urinary excretion of negatively charged 99mTc-labeled multilamellar liposomes, composed of dimyristoylphosphatidylcholine and dimyristoylphosphatidylglycerol in a 7:3 molar ratio, were studied in seven patients with cancer [4].
• Here, we have demonstrated that PGLa is able to assume such an I-state in a 1:1 mixture with magainin 2 at a peptide-to-lipid ratio as low as 1:100 in dimyristoylphosphatidylcholine/dimyristoylphosphatidylglycerol model membranes [5].
• Both N-terminal apoE and the peptide, when complexed with DMPG, competed with (125)I-LDL for binding sites on the surface of cultured human skin fibroblasts [6].
• Thermodynamics of the binding of human apolipoprotein A-I to dimyristoylphosphatidylglycerol [7].
• Analysis of the activation parameters indicates that the interaction of PDC-109 with DMPC membranes is favored by a strong entropic contribution, whereas negative entropic contribution is primarily responsible for the rather weak interaction of this protein with DMPA and DMPG [8].

Biological context of Dimyristoylphosphatidylglycerol

• Similarly, for an equimolar mixture of DPPC and DMPG, we did not observe significant differences in the protein binding for the two phase states [9].
• Time-resolved fluorescence experiments showed that the fluorescence decay of the peptides was best described by double-exponential kinetics, with mean lifetimes values around 8.0 ns in buffer pH 7.4 that increased about 10% in the presence of DMPG vesicles [10].

Anatomical context of Dimyristoylphosphatidylglycerol

• The interaction of two complementary fragments of myelin basic protein from bovine spinal cord with bilayers of dimyristoylphosphatidylglycerol has been studied by broad line 2H and 31P NMR [11].
• The interaction of basic protein from human myelin with dimyristoylphosphatidylglycerol (DMPG) bilayers was investigated by Fourier transform infrared spectroscopy [12].
• Cytochrome c oxidase isolated from beef heart mitochondria was reconstituted in bilayer membranes of the anionic lipid dimyristoylphosphatidylglycerol (DMPG) with varying enzyme/DMPG ratio [13].
• Cation-induced aggregation of acidic phospholipid vesicles consisting of dimyristoylphosphatidylglycerol (DMPG), dipalmitoylphosphatidylserine (DPPS), phosphatidylserine from bovine brain (brPS), and phosphatidylglycerol from egg yolk (eggPG) was studied [14].

Associations of Dimyristoylphosphatidylglycerol with other chemical compounds

• With ferricytochrome c bound to membranes containing a mixture of DMPG (or DOPG) and zwitterionic phosphatidylcholine, the extent of structural perturbation depends on the surface density of the negatively charged lipid head groups, becoming smaller with decreasing proportions of acidic phospholipid in the membrane [15].
• This is in agreement with measurements of tryptophan fluorescence, which show a decrease in quenching efficiency after introduction of DMPG in the lipid system [16].
• Furthermore, NDDP formulated in dimyristoylphosphatidylglycerol (DMPG)-containing liposomes, exhibiting in vitro cytotoxicity comparable to NDDP formulated in PC/Chol/PEG3000-PE liposomes, but showing poor tumor accumulation, was also not effective [17].
• The effect of Na(+) concentration on the subgel phase of dimyristoylphosphatidylglycerol (DMPG) was investigated by differential scanning calorimetry (DSC) and negative stain electron microscopy, and the results were compared with dipalmitoylphosphatidylglycerol (DPPG) [18].
• Membrane vesicles of DMPG anionic lipids containing calcein indicated that gp144 caused a rapid release of fluorescent calcein when interacting with synthetic membranes [19].

Gene context of Dimyristoylphosphatidylglycerol

• However, the motionally restricted lipid population associated with reconstituted cytochrome c oxidase/DMPG membranes increased on binding cytochrome c, indicating structural/dynamic changes taking place in the membrane [13].
• Lipid-protein and protein-protein interactions in double recombinants of myelin proteolipid apoprotein and myelin basic protein with dimyristoylphosphatidylglycerol [20].
• Two-dimensional infrared correlation spectroscopy study of the aggregation of cytochrome c in the presence of dimyristoylphosphatidylglycerol [21].
• Infrared spectra in the CH2 scissoring region indicate that the stable gel phase of DMPG is also characterized by reduced reorientational fluctuations of acyl chains and increased interchain interactions [22].
• For DMPG transfer, we obtained an activation energy of 35 +/- 2 kJ/mol [23].

Analytical, diagnostic and therapeutic context of Dimyristoylphosphatidylglycerol

• DMPG complexes by electron microscopy revealed disc-shaped particles with an average diameter of 13 +/- 3 nm [6].
• This is again in contrast to apo A-I recombinants with DMPG which show no calorimetrically detectable thermal denaturation, at least in a temperature range up to 100 degrees C. Also circular dichroism data indicate high resistance of apo A-I to thermal unfolding in the presence of DMPG [24].
• The interaction of human serum apolipoprotein A-I with dimyristoylphosphatidylglycerol was analyzed by isothermal titration calorimetry [7].
• The thermotropic behavior of dimyristoylphosphatidylglycerol (DMPG) in the absence and presence of cytochrome c under low-salt conditions has been investigated using differential scanning calorimetry (DSC), 31P nuclear magnetic resonance (31P NMR), electron spin resonance (ESR), viscosity, light scattering, and electron microscopy [25].
• By gel filtration chromatography, it is found that protein aggregation is reduced after addition of DMPG to the lipid system [16].

References