PubMed · 15366166
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Nicole Fraser-Hurt, Denise Mabey. 2003. Trachoma.. https://pubmed.ncbi.nlm.nih.gov/15366166/
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Plasma immersion ion implantation (PIII) was used to modify medical-grade PVC coated by triclosan and bronopol to enhance the antibacterial properties. The surface was first activated by O2 plasma to produce more hydrophilic groups so that triclosan and bronopol could be coated more effectively on the surface. Subsequently, an argon plasma treatment was conducted under optimal conditions to improve the antibacterial properties of the triclosan and bronopol-coated PVC samples. The modified surfaces were characterized by XPS, ATR-FTIR, SEM, and contact angle measurements. The antibacterial properties were evaluated utilizing the method of plate-counting of Staphylococcus aureus (gram positive) and Escherichia coli (gram negative). Our experimental results show that the plasma-modified PVC with bronopol exhibits good antibacterial properties while the favorable bulk properties of PVC are retained. The plasma-modified PVC with triclosan has better antibacterial performance against E. coli than bronopol. The change in the antibacterial effect on the modified PVC with time was also investigated and the antibacterial effect was observed to decrease with time.
We report a case of an intravenous drug user who already had a tricuspid bioprosthesis implanted after an infective endocarditis with massive tricuspid regurgitation one year ago. Now he presents with a large mass on the atrial side of the bioprosthesis that led to obstruction; hemocultures contained Enterococcus faecalis. After one-week therapy with antibiotics, aspirin and enoxaparin the mass untangled to a swinging structure and moderate to severe triscupid regurgitation developed; surgery appeared inevitable. After two weeks however the mass was gone, tricuspid insufficiency subsided and the patient became asymptomatic. This case illustrates the potential but controversial role of anticoagulation in the treatment of patients with infective endocarditis.
The winter flounder (Pseudopleuronectes americanus) antimicrobial peptide pleurocidin was produced in Escherichia coli using a synthetic gene constructed by PCR. The gene expresses pleurocidin from pET21a fused to the C-terminus of an insoluble carrier peptide. Once expressed, the fusion peptide formed inclusion bodies in the cytoplasm that were collected, solubilized in guanidine-HCl, and chemically cleaved using hydroxylamine at a unique asparaginyl-glycyl dipeptide. This released recombinant pleurocidin (r-pleurocidin), which was purified using ultrafiltration followed by reverse phase chromatography. The r-pleurocidin peptide resolved as a single band (2.7 kDa) when analyzed by Tris-Tricine buffered SDS-PAGE, and its amino acid sequence was confirmed using tandem mass spectrometry. Extending the pleurocidin sequence with a C-terminal glycine (r-pleurocidin-G) suppressed production of the fusion peptide 15-fold. When pleurocidin was extended further to include aspartate (r-pleurocidin-GD), the same effect was observed, and when pleurocidin was extended with aspartate alone, no effect was observed. Expression of fusion peptide containing either r-pleurocidin-G or r-pleurocidin-GD with low concentrations of inductant caused E. coli to enter stationary phase prematurely, but did not affect overall growth rates. A partial production recovery of r-pleurocidin-G was achieved by inducing expression in stationary phase cells. We observed r-pleurocidin-G to have enhanced antimicrobial activity compared with r-pleurocidin, and we propose that this activity interferes with E. coli metabolism during expression. This antimicrobial effect is probably facilitated by residual solubility of the fusion peptide and by a C-terminal cap structure, which stabilizes the r-pleurocidin-G alpha-helix that is thought to be important for activity.