Lipid Bilayer

Aligned stacks of monomethyl and dimethyl dimyristoyl phosphatidylethanolamine (DMPE) lipid bilayers, like the much studied dimyristoyl PC (DMPC) bilayers, swell anomalously in a critical fashion as the temperature is decreased within the fluid phase towards the main transition temperature, T(M). Unlike DMPC bilayers, both monomethyl and dimethyl DMPE undergo transitions into a gel phase rather than a rippled phase below T(M). Although it is not fully understood why there is anomalous swelling, our present results should facilitate theory by showing that the formation of the phase below T(M) is not related to critical phenomena above T(M).

The conductance and electrostriction of bilayer lipid membranes (sBLM) supported on stainless steel and on conducting polymer polypyrrole (PPY) were studied. We showed that an increase in ammonia concentration resulted in an increase in d.c. current flow across the PPY layer adjacent to the metal surface and that covered by the lipid bilayer. The elasticity modulus in the direction perpendicular to the sBLM surface (E) and the electrical capacitance (C) were characterized by a complicated dependence on the application of an external d.c. voltage. In the case of sBLM formed on the PPY layer and that modified by avidin-urease, higher values of E were observed and in addition the latter system was characterized by a less expressed hysteresis of E and C than the metal supported sBLM. This is evidence that sBLM formed on PPY layers is smoother and more homogeneous than that formed on a metal support. We developed a urea minisensor based on sBLM supported on a PPY layer. Avidin-biotin tec...

The antitumoral effects of oncolytic viruses have generally been limited by inefficient spread of the viruses within infected tumors and by inefficient systemic delivery, particularly in preimmunized hosts. Tumor-selective poxviruses have biolog- ical characteristics that may overcome these limitations. Nevertheless, physical barriers within the tumor microenvi- ronment, including the extracellular matrix, can still limit intratumoral spread, and neutralizing antibodies can

Antimicrobial peptides (AMPs) are showing increasing promise as potential candidate antibacterial drugs in the face of the rapidly emerging bacterial resistance to conventional antibiotics in recent years. The target of these peptides is the microbial membrane and there are numerous models to explain their mechanism of action ranging from pore formation to general membrane disruption. The interaction between the AMP and the target membrane is critical to the specificity and activity of these peptides. However, a precise understanding of the relationship between antimicrobial peptide structure and their cytolytic function in a range of organisms is still lacking. This is a result of the complex nature of the interactions of AMPs with the cell membrane, the mechanism of which can vary considerably between different classes of antimicrobia peptides. A wide range of biophysical techniques have been used to study the influence of a number of peptide and membrane properties on the cytolytic activity of these peptides in model membrane systems. Central to characterisation of this interaction is a quantitative analysis of the binding of peptide to the membrane and the coherent dynamic changes in membrane structure. Recently, dual polarization interferometry has been used to perform an in depth analysis of antimicrobial peptide induced membrane perturbation and with new mass-structure co-fitting kinetic analysis have allowed a real-time label free analysis of binding affinity and kinetics. We review these studies which describe multi-step mechanisms which are adopted by various AMPs in nature and may advance our approach to the development of a new generation of effective antimicrobial therapeutics.