Characterization of the internal morphology of thin film composite membranes used in reverse osmosis (RO) is a prerequisite for understanding the connection between microstructure and water transport properties and is necessary for the design of membranes with improved performance. Here, we examine a series of fully aromatic polyamide active layers of RO membranes that vary in crosslinking using a combination of resonant soft X-ray scattering (RSoXS), transmission electron microscopy (TEM), and atomic force microscopy (AFM). Analysis of RSoXS profiles reveals a correlation between membrane structure and crosslinking density.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
August 2018
As water availability becomes a growing challenge in various regions throughout the world, desalination and wastewater reclamation through technologies such as reverse osmosis (RO) are becoming more important. Nevertheless, many open questions remain regarding the internal structure of thin-film composite RO membranes. In this work, fully aromatic polyamide films that serve as the active layer of state-of-the-art water filtration membranes were investigated using high-angle annular dark-field scanning transmission electron microscopy tomography.
View Article and Find Full Text PDFMiddle East Afr J Ophthalmol
March 2017
We describe a patient with situational restriction of elevation in adduction in his left eye. Clinical examination pointed to instability of the left medial rectus pulley. This was corrected by Faden on the medial rectus.
View Article and Find Full Text PDFNat Clin Pract Cardiovasc Med
March 2006
Advances in immunosuppression, guided by invasive endomyocardial biopsy for the assessment of graft rejection, have ushered heart transplantation into the clinical arena by the demonstration of acceptable 1-year outcomes. Further decreases in the risk of malignancy and cardiac allograft vasculopathy that improve long-term outcomes, are, however, still desired. Attention has become directed towards the use of markers that can be detected noninvasively to provide insight into underlying molecular and cellular events associated with the immune response and graft function.
View Article and Find Full Text PDFOmpT is a surface protease of gram-negative bacteria that has been shown to cleave antimicrobial peptides, activate human plasminogen, and degrade some recombinant heterologous proteins. We have analyzed the substrate specificity of OmpT by two complementary substrate filamentous phage display methods: (i) in situ cleavage of phage that display protease-susceptible peptides by Escherichia coli expressing OmpT and (ii) in vitro cleavage of phage-displayed peptides using purified enzyme. Consistent with previous reports, OmpT was found to exhibit a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position (P1 and P1' are the residues immediately prior to and following the scissile bond).
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