Anisotropy in mechanical properties and fracture behavior of an oxide dispersion Fe20Cr5Al alloy

Anisotropy of fracture toughness and fracture behavior of Fe20Cr5Al oxide dispersion-strengthened alloy has been investigated by means of compression tests, hardness tests, and wedge splitting test. The results show a small effect of the compression direction on yield strength (YS) and strain hardening. The YS is minimum for longitudinal direction and maximum for the tangential direction. The transverse plastic strain ratio is similar for tangential and longitudinal directions but very different from that in normal direction. Hardness depends on the indentation plane; it is lower for any plane parallel to the L-T plane and of similar magnitude for the other orthogonal planes, i.e., the L-S and T-S planes. Macroscopically, two failure modes have been observed after wedge-splitting tests, those of LS and TS specimens in which fracture deviates along one or two branches normal to the notch plane, and those of LT, TL, SL, and ST specimens in which fracture propagates along the notch plane. Besides LT and TL specimens present delaminations parallel to L-T plane. Both, the fracture surface of branching cracks and that of the delaminations, show an intergranular brittle fracture appearance. It is proposed that the main cause of the delamination and crack branching is the alignment in the mesoscopic scale of the ultrafine grains structure which is enhanced by the 〈110〉- texture of the material and by the presence in the grain boundaries of both yttria dispersoids and impurity contaminations. An elastoplastic finite element analysis was performed to study what stress state is the cause of the branches and delaminations. It is concluded that the normal to the crack branches and/or the shear stress components could determine the crack bifurcation mechanism, whereas the delamination it seems that it is controlled by the magnitude of the stress component normal to the delamination plane. © The Minerals, Metals & Materials Society and ASM International 2014.Peer Reviewe

A peptide derived from TIMP-3 inhibits multiple angiogenic growth factor receptors and tumour growth and inflammatory arthritis in mice

The binding of vascular endothelial growth factor (VEGF) to VEGF receptor-2 (VEGFR-2) on the surface of vascular endothelial cells stimulates many steps in the angiogenic pathway. Inhibition of this interaction is proving of value in moderating the neovascularization accompanying age-related macular degeneration and in the treatment of cancer. Tissue inhibitor of metalloproteinases-3 (TIMP-3) has been shown to be a natural VEGFR-2 specific antagonist—an activity that is independent of its ability to inhibit metalloproteinases. In this investigation we localize this activity to the C-terminal domain of the TIMP-3 molecule and characterize a short peptide, corresponding to part of this domain, that not only inhibits all three VEGF-family receptors, but also fibroblast growth factor and platelet-derived growth factor receptors. This multiple-receptor inhibition may explain why the peptide was also seen to be a powerful inhibitor of tumour growth and also a partial inhibitor of arthritic joint inflammation in vivo

DsbL and DsbI form a specific dithiol oxidase system for periplasmic arylsulfate sulfotransferase in uropathogenic Escherichia coli

Disulfide bond formation in the Escherichia coli periplasm requires the transfer of electrons from substrate proteins to DsbA, which is recycled as an oxidant by the membrane protein DsbB. The highly virulent, uropathogenic E. coli strain CFT073 contains a second, homologous pair of proteins, DsbL and DsbI, which are encoded in a tri-cistronic operon together with a periplasmic, uropathogen-specific arylsulfate sulfotransferase (ASST). We show that DsbL and DsbI form a functional redox pair, and that ASST is a substrate of DsbL/DsbI in vivo. DsbL is the most reactive oxidizing thioredoxin-like protein known to date. In contrast to DsbA, however, DsbL oxidizes reduced RNaseA with a much lower rate and prevents unspecific aggregation of reduced insulin. The 1.55 A resolution crystal structure of reduced DsbL provides insight into the reduced state of thioredoxin-like dithiol oxidases at high resolution, and reveals an unusual cluster of basic residues stabilizing the thiolate anion of the nucleophilic active-site cysteine. We propose that the DsbL/DsbI pair of uropathogenic E. coli was acquired as an additional, specific redox couple that guarantees biological activity of ASST