Automatització de la configuració de dispositius de xarxa basat en mapeig de ontologies

Actualment, hi ha un problema dins del m´on d’internet, concretament a la capa IP (capa 3). Qualsevol gesti´o que es vulgui fer dins d’aquesta capa, s’ha de fer de forma manual, cosa que implica que l’encarregat de la gesti´o hagi de con`eixer moltes comandes de configuraci´o d’un router, i possiblement comandes equivalents per a routers diferents. Dins d’aquest projecte es vol millorar i simplificar la gesti´o de routers. M´es concretament, es crea una aplicaci´o que permeti a l’usuari final executar una configuraci ´o havent d’introduir tan sols els valors d’entrada necessaris. Mentre que avui en dia per crear un link IP entre dos routers s’ha de primer configurar un router de forma manual, i despr´es l’altre, amb aquest projecte es pot a partir dels valors introdu¨ıts construir els arxius que permetin llanc¸ar la configuraci´o de forma autom`atica i executar-los. Per a fer aix`o, s’utilitza per una banda una aplicaci´o de gesti´o de xarxes, l’OpenNMS, per a saber quins dispositius es t´e disponibles, que es puguin veure, i que es puguin configurar. A m´es, s’utilitzen una s`erie d’ontologies que guarden, entre d’altres, el conjunt de comandes disponibles de cara a la configuraci´o. Finalment, es proposa una IA que permeti a partir d’una ordre, entendre el que es demana. A partir d’aix`o, es permetria convertir aquesta ordre en instruccions concretes amb les eines i amb la implementaci´o ja mencionada. Aquest projecte est`a dins del marc de ONE, un projecte col·laboratiu a nivell internacional, format per diverses empreses i universitats, entre les quals hi ha la Universitat Polit`ecnica de Catalunya1. De fet, ja hi ha hagut una presentaci´o dins d’aquest mateix marc mostrant aquest projecte, on els assistents han pogut veure la configuraci´o autom`atica de dos routers per tal de crear un link IP

Investigations of tethered bilayer lipid membranes for their potential use in biosensing devices

Tethered bilayer lipid membranes (tBLMs) provide a model platform for the investigation ofvarious membrane related processes. They are especially suited to study the incorporation and function of ion channel proteins, where a high background resistance ofthe membrane is essential. In this study, the electrochemical sealing properties ofnew tBLMs are characterised and improved. Membranes of different compositions have been studied for their ability to host ion channels using Surface Plasmon Resonance Spectroscopy (SPR) and Electrochemical Impedance Spectroscopy (EIS). Several membrane proteins such as carriers, channels and pores were functionally incorporated. and investigated in different tBLM architectures. As a first test of the functionality of the membrane assembly the carrier valinomycin and the channel gramicidin were incorporated and their ion selectivity demonstrated with EIS. The transmembrane fragment M2 of the nicotinic acetylcholine receptor (nAChR) was embedded into a tBLM by fusion of proteoliposomes with different monolayers. The pore was selective for small monovalent cations, while bulky ions could not pass the membrane. The tBLMs provide a platfonn for the study of ion transport phenomena and ligand interactions of channels such as the nAChR, as the presented method should be generally applicable to other membrane proteins. Incorporation of a-haemolysin, a toxin that leads to lysis of cells by formation of large pores in the cell m,e. mbrane, was achieved. The tBLM provides a fluidity that allows incorporating the pores, while at the same time providing a submembrane space between the solid support and the bilayer. This offers the ability to measure ion currents through the incorporated channels. A membrane architecture specially suited for an enhanced functionality ofthe pores was designed and characterised. Downsizing the membrane area on Jl-electrodes gave gigaohmic membrane resistances, showing sealing properties comparable to BLMs. This gigaseal allowed for highly f sensitive measurements ofcurrents through incorporated a-haemolysin pores. With this system, a biosensor with modified biological receptors as actual sensing units is feasible, whereas the high stability opens the perspective of long-term experiments and continuous monitoring. Thus, a major step towards the use of proteins as stochastic sensing elements in prospective biosensor applications has been accomplished.EThOS - Electronic Theses Online ServiceGBUnited Kingdo

Impedance Analysis of Complex Formation Equilibria in Phosphatidylcholine Bilayers Containing Decanoic Acid or Decylamine

Bilayer lipid membranes composed of phosphatidylcholine and decanoic acid or phosphatidylcholine and decylamine were investigated using electrochemical impedance spectroscopy. Interaction between membrane components causes significant deviations from the additivity rule. Area, capacitance, and stability constant values for the complexes were calculated based on the model assuming 1:1 stoichiometry, and the model was validated by comparison of these values to experimental results. We established that phosphatidylcholine and decylamine form highly stable 1:1 complexes. In the case of decanoic acid-modified phosphatidylcholine membranes, complexes with stoichiometries other than 1:1 should be taken into consideration

Membrane Association of the PTEN Tumor Suppressor: Molecular Details of the Protein-Membrane Complex from SPR Binding Studies and Neutron Reflection

The structure and function of the PTEN phosphatase is investigated by studying its membrane affinity and localization on in-plane fluid, thermally disordered synthetic membrane models. The membrane association of the protein depends strongly on membrane composition, where phosphatidylserine (PS) and phosphatidylinositol diphosphate (PI(4,5)P2) act pronouncedly synergistic in pulling the enzyme to the membrane surface. The equilibrium dissociation constants for the binding of wild type (wt) PTEN to PS and PI(4,5)P2 were determined to be Kd∼12 µM and 0.4 µM, respectively, and Kd∼50 nM if both lipids are present. Membrane affinities depend critically on membrane fluidity, which suggests multiple binding sites on the protein for PI(4,5)P2. The PTEN mutations C124S and H93R show binding affinities that deviate strongly from those measured for the wt protein. Both mutants bind PS more strongly than wt PTEN. While C124S PTEN has at least the same affinity to PI(4,5)P2 and an increased apparent affinity to PI(3,4,5)P3, due to its lack of catalytic activity, H93R PTEN shows a decreased affinity to PI(4,5)P2 and no synergy in its binding with PS and PI(4,5)P2. Neutron reflection measurements show that the PTEN phosphatase “scoots" along the membrane surface (penetration <5 Å) but binds the membrane tightly with its two major domains, the C2 and phosphatase domains, as suggested by the crystal structure. The regulatory C-terminal tail is most likely displaced from the membrane and organized on the far side of the protein, ∼60 Å away from the bilayer surface, in a rather compact structure. The combination of binding studies and neutron reflection allows us to distinguish between PTEN mutant proteins and ultimately may identify the structural features required for membrane binding and activation of PTEN

Ion Channels in Tethered Bilayer Lipid Membranes on Au Electrodes

New York, US

The formation of tethered bilayer lipid membranes probed by various surface sensitive techniques

100 PARK DR, STE 105, CALLER BOX 13994, RESEARCH TRIANGLE PARK, USA, NC, 2770

An Investigation of the Complexity of Maillard Reaction Product Profiles from the Thermal Reaction of Amino Acids with Sucrose Using High Resolution Mass Spectrometry

Thermal treatment of food changes its chemical composition drastically with the formation of “so-called” Maillard reaction products, being responsible for the sensory properties of food, along with detrimental and beneficial health effects. In this contribution, we will describe the reactivity of several amino acids, including arginine, lysine, aspartic acid, tyrosine, serine and cysteine, with carbohydrates. The analytical strategy employed involves high and ultra-high resolution mass spectrometry followed by chemometric-type data analysis. The different reactivity of amino acids towards carbohydrates has been observed with cysteine and serine, resulting in complex MS spectra with thousands of detectable reaction products. Several compounds have been tentatively identified, including caramelization reaction products, adducts of amino acids with carbohydrates, their dehydration and hydration products, disproportionation products and aromatic compounds based on molecular formula considerations