Controllable Synthesis of Single-Crystalline CdO and Cd(OH)2Nanowires by a Simple Hydrothermal Approach

Single-crystalline Cd(OH)2 or CdO nanowires can be selectively synthesized at 150 °C by a simple hydrothermal method using aqueous Cd(NO3)2 as precursor. The method is biosafe, and compared to the conventional oil-water surfactant approach, more environmental-benign. As revealed by the XRD results, CdO or Cd(OH)2 nanowires can be generated in high purity by varying the time of synthesis. The results of FESEM and HRTEM analysis show that the CdO nanowires are formed in bundles. Over the CdO-nanowire bundles, photoluminescence at ~517 nm attributable to near band-edge emission of CdO was recorded. Based on the experimental results, a possible growth mechanism of the products is proposed

Engineering Porous Poly(lactic acid) Scaffolds with High Mechanical Performance via a Solid State Extrusion/Porogen Leaching Approach

A knotty issue concerning the poor mechanical properties exists in the porogen leaching approach to porous scaffolds, despite its advantage in tuning pore structure. To address this hurdle, solid state extrusion (SSE) combined with porogen leaching was utilized to engineer porous scaffolds of poly(lactic acid) (PLA). Advances introduced by poly(ethylene glycol) (PEG) caused the PLA ductile to be processed and, on the other hand, enabled the formation of interconnected pores. Thus, a well-interconnected porous architecture with high connectivity exceeding 97% and elevated porosity over 60% was obtained in the as-prepared PLA scaffolds with the composition of NaCl higher than 75.00 wt % and PEG beyond 1.25 wt %. More strikingly, the pore walls of macropores encompassed countless micropores and rough surface topography, in favor of transporting nutrients and metabolites as well as cell attachment. The prominent compressive modulus of the PLA scaffolds was in the range of 85.7–207.4 MPa, matching the normal modulus of human trabecular bone (50–250 MPa). By means of alkaline modification to improve hydrophilicity, biocompatible porous PLA scaffolds exhibited good cell attachment. These results suggest that the SSE/porogen leaching approach provides an eligible clue for fabricating porous scaffolds with high mechanical performance for use as artificial extracellular matrices

Mechanisms Involved in the Functional Divergence of Duplicated GroEL Chaperonins in <em>Myxococcus xanthus</em> DK1622

<div><p>The gene encoding the GroEL chaperonin is duplicated in nearly 30% of bacterial genomes; and although duplicated <i>groEL</i> genes have been comprehensively determined to have distinct physiological functions in different species, the mechanisms involved have not been characterized to date. <i>Myxococcus xanthus</i> DK1622 has two copies of the <i>groEL</i> gene, each of which can be deleted without affecting cell viability; however, the deletion of either gene does result in distinct defects in the cellular heat-shock response, predation, and development. In this study, we show that, from the expression levels of different <i>groELs</i>, the distinct functions of <i>groEL1</i> and <i>groEL2</i> in predation and development are probably the result of the substrate selectivity of the paralogous GroEL chaperonins, whereas the lethal effect of heat shock due to the deletion of <i>groEL1</i> is caused by a decrease in the total <i>groEL</i> expression level. Following a bioinformatics analysis of the composition characteristics of GroELs from different bacteria, we performed region-swapping assays in <i>M. xanthus</i>, demonstrating that the differences in the apical and the C-terminal equatorial regions determine the substrate specificity of the two GroELs. Site-directed mutagenesis experiments indicated that the GGM repeat sequence at the C-terminus of GroEL1 plays an important role in functional divergence. Divergent functions of duplicated GroELs, which have similar patterns of variation in different bacterial species, have thus evolved mainly via alteration of the apical and the C-terminal equatorial regions. We identified the specific substrates of strain DK1622's GroEL1 and GroEL2 using immunoprecipitation and mass spectrometry techniques. Although 68 proteins bound to both GroEL1 and GroEL2, 83 and 46 proteins bound exclusively to GroEL1 or GroEL2, respectively. The GroEL-specific substrates exhibited distinct molecular sizes and secondary structures, providing an encouraging indication for GroEL evolution for functional divergence.</p> </div