Values of the bending modulus KC are reviewed, and possible causes for the considerable differences are discussed. One possible cause is the use of glucose and sucrose in the classical micromechanical manipulation and shape analysis methods. New data, using the more recent low angle x-ray method, are presented that do not support an effect of glucose or sucrose on KC. Another possible cause is using an incomplete theory to interpret the data. Adding a tilt term to the theory clearly does not affect the value obtained from the shape analysis method. It is shown that a tilt term, using a value of the modulus Kθ indicated by simulations, theory, and estimated from order parameters obtained from NMR and from the wide angle x-ray method, should also not affect the value obtained using the micromechanical manipulation method, although it does require a small correction when determining the value of the area compressibility modulus KA. It is still being studied whether including a tilt term will significantly affect the values of KC obtained using low angle x-ray data. It remains unclear what causes the differences in the experimental values of KC for simple lipid bilayers.
High resolution structure is presented for the ripple (Pβ′) phase of the phospholipid dimyristoylphosphatidylcholine. Low angle X-ray scattering from oriented samples yielded 57 orders, more than twice as many as recorded previously. The determined electron density map has a sawtooth profile similar to the result from lower resolution data, but the features are sharper allowing better estimates for the modulated bilayer profile and the distribution of headgroups along the aqueous interface. Analysis of high resolution wide angle X-ray data shows that the hydrocarbon chains in the longer, major side of the asymmetric sawtooth are packed similarly to the LβF gel phase, with chains in both monolayers coupled and tilted by 18° in the same direction. The absence of Bragg rods that could be associated with the minor side is consistent with disordered chains, as often suggested in the literature. However, the new high resolution bilayer profile strongly suggests that the chains in the two monolayers in the minor side and the curved region are not in registry. This staggered monolayer modulated melting suggests a direction for improving theories of the ripple phase.
Recent simulations have indicated that the traditional model for topographical fluctuations in biomembranes should be enriched to include molecular tilt. Here we report the first experimental data supporting this enrichment. Utilizing a previously posited tilt-dependent model, a height-height correlation function was derived. The x-ray scattering from a liquid crystalline stack of oriented fluid phase lipid bilayers was calculated and compared with experiment. By fitting the measured scattering intensity, both the bending modulus K(c)=8.3±0.6×10⁻²⁰ J and the tilt modulus K(θ)=95±7 mN/m were determined for DOPC lipid bilayers at 30 °C.
We report the effect on lipid bilayers of the Tat peptide Y47GRKKRRQRRR57 from the HIV-1 virus transactivator of transcription (Tat) protein. Synergistic use of low-angle X-ray scattering (LAXS) and atomistic molecular dynamics simulations (MD) indicate Tat peptide binding to neutral dioleoylphosphocholine (DOPC) lipid headgroups. This binding induced the local lipid phosphate groups to move 3 Å closer to the center of the bilayer. Many of the positively charged guanidinium components of the arginines were as close to the center of the bilayer as the locally thinned lipid phosphate groups. LAXS data for DOPC, DOPC/dioleoylphosphoethanolamine (DOPE), DOPC/dioleoylphosphoserine (DOPS), and a mimic of the nuclear membrane gave similar results. Generally, the Tat peptide decreased the bilayer bending modulus KC and increased the area/lipid. Further indications that Tat softens a membrane, thereby facilitating translocation, were provided by wide-angle X-ray scattering (WAXS) and neutron scattering. CD spectroscopy was also applied to further characterize Tat/membrane interactions. Although a mechanism for translocation remains obscure, this study suggests that the peptide/lipid interaction makes the Tat peptide poised to translocate from the headgroup region.
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