High impact information on dimyristoylphosphatidylserine

• In anionic membranes of dimyristoylphosphatidylglycerol and dimyristoylphosphatidylserine, both HSP17 and alpha-crystallin strongly stabilize the liquid-crystalline state [1].
• DMPS with saturated acyl chains was found to be a much more potent transport enhancer than those with unsaturated acyl chains (DOPS and DOPG) [2].
• With the aim of establishing acidic bicellar solutions as a useful membrane model system, we have used deuterium NMR spectroscopy to investigate the properties of dimyristoyl/dihexanoylphosphatidylcholine (DMPC/DHPC) bicelles containing 25% (w/w in H(2)O) of either dimyristoylphosphatidylserine (DMPS) or dimyristoylphosphatidylglycerol (DMPG) [3].
• CD spectra of the peptides indicated that NM-peptide underwent a dramatic structural change in the presence of dimyristoylphosphatidylserine (DMPS) vesicles, whereas spectra acquired in PC7 micelles were similar to those acquired in buffer alone [4].
• Human erythrocytes were incubated with sonicated vesicles composed of diheptanoyl-, dioctanoyl-, didecanoyl-, or dimyristoylphosphatidylserine, and the transbilayer distribution of the incorporated foreign lipid was examined by monitoring changes in cell morphology (Daleke & Huestis (1989) J. Cell. Biol. 108, 1375) [5].

Associations of dimyristoylphosphatidylserine with other chemical compounds

• Deuterium nuclear magnetic resonance (2H NMR) was used to study the interaction of cytochrome c (from horse heart) with bilayers of mixed dimyristoylphosphatidylcholine (DMPC) and dimyristoylphosphatidylserine (DMPS) [6].
• In addition, we report the unexpected observation that prothrombin increased the anisotropy of DPH in DMPS/DMPC vesicles in the liquid-crystalline phase in the absence of Ca2+ as well as in its presence [7].
• On protonation of the carboxyl group (pK2app = 5.5), the transition temperature increases from 36 to 44 degrees C in the fully hydrated state of dimyristoylphosphatidylserine (from 54 to 62 degrees C for dipalmitoylphosphatidylserine), at ionic strength J = 0 [8].
• Dynamics and ordering in mixed model membranes of dimyristoylphosphatidylcholine and dimyristoylphosphatidylserine: a 250-GHz electron spin resonance study using cholestane [9].
• The interaction of alpha-tocopherol with dimyristoylphosphatidylserine (DMPS) has been studied in the presence and in the absence of Ca2+ by using differential scanning calorimetry (DSC), Fourier transform infrared spectroscopy (FT-IR) and 45Ca2+-binding [10].

Gene context of dimyristoylphosphatidylserine

• The binding of either drug to DMPS resulted in an increased pressure required to halt the reorientational fluctuations of the acyl chains, indicating that the distance between the chains were increased [11].
• Second, the effect of rhodopsin incorporation on the dimyristoylphosphatidylserine (DMPS) gel to liquid-crystalline phase transition was analyzed with ESR techniques [12].

Analytical, diagnostic and therapeutic context of dimyristoylphosphatidylserine

• The selectivity of the DMPS/spectrin interaction is established by quantitative evaluation of the shifts of the phase boundaries (liquidus and solidus line) caused by the lipid/protein interaction as a function of the composition of the binary lipid mixtures [13].

References