2 research outputs found
One-Pot Synthesis of Pyrrole-2-carboxylates and -carboxamides via an Electrocyclization/Oxidation Sequence
An electrocyclic ring closure is
the key step of an efficient one-pot
method for the synthesis of pyrrole-2-carboxylates and -carboxamides
from chalcones and glycine esters or amides. The 3,4-dihydro-2<i>H</i>-pyrrole intermediates generated in situ are oxidized to
the corresponding pyrroles by stoichiometric oxidants or by catalytic
copperÂ(II) and air in moderate to high yields. A wide range of functional
groups are tolerated, and further combination with an in situ bromination
gives access to polyfunctional pyrrole scaffolds
Image_1_The Staphylococcus aureus Extracellular Adherence Protein Eap Is a DNA Binding Protein Capable of Blocking Neutrophil Extracellular Trap Formation.PDF
<p>The extracellular adherence protein (Eap) of Staphylococcus aureus is a secreted protein known to exert a number of adhesive and immunomodulatory properties. Here we describe the intrinsic DNA binding activity of this multifunctional secretory factor. By using atomic force microscopy, we provide evidence that Eap can bind and aggregate DNA. While the origin of the DNA substrate (e.g., eukaryotic, bacterial, phage, and artificial DNA) seems to not be of major importance, the DNA structure (e.g., linear or circular) plays a critical role with respect to the ability of Eap to bind and condense DNA. Further functional assays corroborated the nature of Eap as a DNA binding protein, since Eap suppressed the formation of “neutrophil extracellular traps” (NETs), composed of DNA-histone scaffolds, which are thought to function as a neutrophil-mediated extracellular trapping mechanism. The DNA binding and aggregation activity of Eap may thereby protect S. aureus against a specific anti-microbial defense reaction from the host.</p