Glucosyl anthranilate

In the crystal structure of the title compound, C21H25NO11, the hexopyranosyl ring adopts a chair conformation and the five substituents are in equatorial positions. An intra­molecular hydrogen bond between the amino group and a neighbouring carbonyl group is found. Two carbonyl groups are disordered and were refined using a split model

Magnetoresistance in Thin Permalloy Film (10nm-thick and 30-200nm-wide) Nanocontacts Fabricated by e-Beam Lithography

In this paper we show spin dependent transport experiments in nanoconstrictions ranging from 30 to 200nm. These nanoconstrictions were fabricated combining electron beam lithography and thin film deposition techniques. Two types of geometries have been fabricated and investigated. We compare the experimental results with the theoretical estimation of the electrical resistance. Finally we show that the magnetoresistance for the different geometries does not scale with the resistance of the structure and obtain drops in voltage of 20mV at 20Oe.Comment: 15 pages, 4 figures. Accepted by AP

Pseudomonas aeruginosa Elastase Provides an Escape from Phagocytosis by Degrading the Pulmonary Surfactant Protein-A

Pseudomonas aeruginosa is an opportunistic pathogen that causes both acute pneumonitis in immunocompromised patients and chronic lung infections in individuals with cystic fibrosis and other bronchiectasis. Over 75% of clinical isolates of P. aeruginosa secrete elastase B (LasB), an elastolytic metalloproteinase that is encoded by the lasB gene. Previously, in vitro studies have demonstrated that LasB degrades a number of components in both the innate and adaptive immune systems. These include surfactant proteins, antibacterial peptides, cytokines, chemokines and immunoglobulins. However, the contribution of LasB to lung infection by P. aeruginosa and to inactivation of pulmonary innate immunity in vivo needs more clarification. In this study, we examined the mechanisms underlying enhanced clearance of the ΔlasB mutant in mouse lungs. The ΔlasB mutant was attenuated in virulence when compared to the wild-type strain PAO1 during lung infection in SP-A+/+ mice. However, the ΔlasB mutant was as virulent as PAO1 in the lungs of SP-A-/- mice. Detailed analysis showed that the ΔlasB mutant was more susceptible to SP-A-mediated opsonization but not membrane permeabilization. In vitroand in vivo phagocytosis experiments revealed that SP-A augmented the phagocytosis of ΔlasB mutant bacteria more efficiently than the isogenic wild-type PAO1. The ΔlasB mutant was found to have a severely reduced ability to degrade SP-A, consequently making it unable to evade opsonization by the collectin during phagocytosis. These results suggest that P. aeruginosa LasB protects against SP-A-mediated opsonization by degrading the collectin