Graph measures and network robustness

Network robustness research aims at finding a measure to quantify network robustness. Once such a measure has been established, we will be able to compare networks, to improve existing networks and to design new networks that are able to continue to perform well when it is subject to failures or attacks. In this paper we survey a large amount of robustness measures on simple, undirected and unweighted graphs, in order to offer a tool for network administrators to evaluate and improve the robustness of their network. The measures discussed in this paper are based on the concepts of connectivity (including reliability polynomials), distance, betweenness and clustering. Some other measures are notions from spectral graph theory, more precisely, they are functions of the Laplacian eigenvalues. In addition to surveying these graph measures, the paper also contains a discussion of their functionality as a measure for topological network robustness

Preferential adsorption of high density lipoprotein (HDL) in blood plasma/polymer interaction

A few studies on the adsorption of plasma proteins to polymeric surfaces show that major plasma proteins: albumin (Alb), fibrinogen (Fb) and immunoglobulin (IgG) are adsorbed in much smaller quantities from plasma than from protein solutions (1,2). Present results show that this difference in adsorption is due to the preferential adsorption of high density lipoprotein from plasma onto the material surfaces studied (PVC and PS)

Context-Independent Centrality Measures Underestimate the Vulnerability of Power Grids

Power grids vulnerability is a key issue in society. A component failure may trigger cascades of failures across the grid and lead to a large blackout. Complex network approaches have shown a direction to study some of the problems faced by power grids. Within Complex Network Analysis structural vulnerabilities of power grids have been studied mostly using purely topological approaches, which assumes that flow of power is dictated by shortest paths. However, this fails to capture the real flow characteristics of power grids. We have proposed a flow redistribution mechanism that closely mimics the flow in power grids using the PTDF. With this mechanism we enhance existing cascading failure models to study the vulnerability of power grids. We apply the model to the European high-voltage grid to carry out a comparative study for a number of centrality measures. `Centrality' gives an indication of the criticality of network components. Our model offers a way to find those centrality measures that give the best indication of node vulnerability in the context of power grids, by considering not only the network topology but also the power flowing through the network. In addition, we use the model to determine the spare capacity that is needed to make the grid robust to targeted attacks. We also show a brief comparison of the end results with other power grid systems to generalise the result.Comment: Pre-Proceedings of CRITIS '1

Distributed flow optimization and cascading effects in weighted complex networks

We investigate the effect of a specific edge weighting scheme $\sim (k_i k_j)^{\beta}$ on distributed flow efficiency and robustness to cascading failures in scale-free networks. In particular, we analyze a simple, yet fundamental distributed flow model: current flow in random resistor networks. By the tuning of control parameter $\beta$ and by considering two general cases of relative node processing capabilities as well as the effect of bandwidth, we show the dependence of transport efficiency upon the correlations between the topology and weights. By studying the severity of cascades for different control parameter $\beta$, we find that network resilience to cascading overloads and network throughput is optimal for the same value of $\beta$ over the range of node capacities and available bandwidth

Biophysical Characterization and Membrane Interaction of the Two Fusion Loops of Glycoprotein B from Herpes Simplex Type I Virus

The molecular mechanism of entry of herpesviruses requires a multicomponent fusion system. Cell invasion by Herpes simplex virus (HSV) requires four virally encoded glycoproteins: namely gD, gB and gH/gL. The role of gB has remained elusive until recently when the crystal structure of HSV-1 gB became available and the fusion potential of gB was clearly demonstrated. Although much information on gB structure/function relationship has been gathered in recent years, the elucidation of the nature of the fine interactions between gB fusion loops and the membrane bilayer may help to understand the precise molecular mechanism behind herpesvirus-host cell membrane fusion. Here, we report the first biophysical study on the two fusion peptides of gB, with a particular focus on the effects determined by both peptides on lipid bilayers of various compositions. The two fusion loops constitute a structural subdomain wherein key hydrophobic amino acids form a ridge that is supported on both sides by charged residues. When used together the two fusion loops have the ability to significantly destabilize the target membrane bilayer, notwithstanding their low bilayer penetration when used separately. These data support the model of gB fusion loops insertion into cholesterol enriched membranes

Controlled Release from Cleavable Polymerized Liposomes upon Redox and pH Stimulation

A gallate derivative with three propargyl groups was coupled to palmitoyl oleoyl phosphoethanolamine (POPE). The resulting anionic lipid was formulated with common lipids such as palmitoyl oleoyl phosphatidyl choline (POPC) to form large unilamellar vesicles (LUVs). Polymerization of the LUVs was accomplished by the Cu(I)-catalyzed click reaction between the propargyl groups and the azide groups in the cross-linker. When the cross-linker contained a disulfide or ketal group, the resulting polymerized liposomes depolymerized and released entrapped contents upon the addition of a reducing thiol or under weakly acidic conditions. The click reaction allowed simultaneous multivalent surface functionalization during cross-linking, making these cleavable polymerized liposomes (CPLs) potentially very useful in the delivery and controlled release of pharmaceutical agents

Tuning Curvature and Stability of Monoolein Bilayers by Designer Lipid-Like Peptide Surfactants

This study reports the effect of loading four different charged designer lipid-like short anionic and cationic peptide surfactants on the fully hydrated monoolein (MO)-based Pn3m phase (Q224). The studied peptide surfactants comprise seven amino acid residues, namely A6D, DA6, A6K, and KA6. D (aspartic acid) bears two negative charges, K (lysine) bears one positive charge, and A (alanine) constitutes the hydrophobic tail. To elucidate the impact of these peptide surfactants, the ternary MO/peptide/water system has been investigated using small-angle X-ray scattering (SAXS), within a certain range of peptide concentrations (R≤0.2) and temperatures (25 to 70°C). We demonstrate that the bilayer curvature and the stability are modulated by: i) the peptide/lipid molar ratio, ii) the peptide molecular structure (the degree of hydrophobicity, the type of the hydrophilic amino acid, and the headgroup location), and iii) the temperature. The anionic peptide surfactants, A6D and DA6, exhibit the strongest surface activity. At low peptide concentrations (R = 0.01), the Pn3m structure is still preserved, but its lattice increases due to the strong electrostatic repulsion between the negatively charged peptide molecules, which are incorporated into the interface. This means that the anionic peptides have the effect of enlarging the water channels and thus they serve to enhance the accommodation of positively charged water-soluble active molecules in the Pn3m phase. At higher peptide concentration (R = 0.10), the lipid bilayers are destabilized and the structural transition from the Pn3m to the inverted hexagonal phase (H2) is induced. For the cationic peptides, our study illustrates how even minor modifications, such as changing the location of the headgroup (A6K vs. KA6), affects significantly the peptide's effectiveness. Only KA6 displays a propensity to promote the formation of H2, which suggests that KA6 molecules have a higher degree of incorporation in the interface than those of A6K