Lifetime Comparisons of Organic Light-Emitting Diodes Fabricated by Solution and Evaporation Processes.

In this paper, a blue fluorescent organic light-emitting diode (OLED) with a 1 cm2 emitting area was fabricated by a solution process. The ITO/spin MADN:13% UBD-07/TPBi/Al was used as the basic structure in which to add a hole-injection layer PEDOT:PSS and an electron-injection layer LiF, respectively. The device structure was optimized to obtain a longer lifetime. Firstly, the TPBi, which is an electron transport layer and a hole-blocking layer, was added to the structure to increase the electron transport rate. When the TPBi thickness was increased to 20 nm, the luminance was 221 cd/m2, and the efficiency was 0.52 cd/A at a voltage of 8 V. Since the addition of the hole-injection layer (HIL) increased the hole current but did not increase the electron current, the electron transport layer (ETL) Alq3 with the lowest unoccupied molecular orbital (LUMO) was added as stepped ETL to help the TPBi transport more electron current into the emitting layer. When the thickness of the TPBi/Alq3 was 10 nm/15 nm, the luminance reached 862 cd/m2, the efficiency was 1.29 cd/A, and the lifetime increased to 252 min. Subsequently, a hole-injection layer PEDOT:PSS with a thickness of 55 nm was added to make the ITO surface flatter and to reduce the probability of a short circuit caused by the spike effect. At this time, the luminance of 311 cd/m2, the efficiency of 0.64 cd/A, and the lifetime of 121 min were obtained. Following this, the thickness of the emitting layer was doubled to increase the recombination probability of the electrons and the holes. When the thickness of the emitting layer was 90 nm, and the thermal evaporation method was used, the efficiency was 3.23 cd/A at a voltage of 8V, and the lifetime was improved to 482 min. Furthermore, when the thickness of the hole-injection layer PEDOT:PSS was increased to 220 nm, the efficiency increased to 3.86 cd/A, and the lifetime was increased to 529 min. An infrared thermal image camera was employed to detect the temperature variation of the blue OLEDs. After the current was gradually increased, it was found that the heat accumulation of the device became more and more significant. When the driving current reached 50 mA, the device burnt out. It was found that the maximum temperature that the OLED device could withstand was approximately 58.83 degrees C at a current of 36.36 mA.

Easy strategy to increase salt resistance of antimicrobial peptides.

The efficacies of many antimicrobial peptides are greatly reduced under high salt concentrations, limiting their development as pharmaceutical compounds. Here, we describe an easy strategy to increase salt resistance of antimicrobial peptides by replacing tryptophan or histidine residues with the bulky amino acids ß-naphthylalanine and ß-(4,4'-biphenyl)alanine. The activities of the salt-sensitive peptide P-113 were diminished at high salt concentrations, whereas the activities of its ß-naphthylalanine and ß-(4,4'-biphenyl)alanine-substituted variant were less affected.

Rational design of tryptophan-rich antimicrobial peptides with enhanced antimicrobial activities and specificities.

Trp-rich antimicrobial peptides play important roles in the host innate defense mechanism of many plants and animals. A series of short Trp-rich peptides derived from the C-terminal region of Bothrops asper myothoxin II, a Lys49 phospholipase A(2) (PLA(2)), were found to reproduce the antimicrobial activities of their parent molecule. Of these peptides, KKWRWWLKALAKK-designated PEM-2-was found to display improved activity against both Gram-positive and Gram-negative bacteria. To improve the antimicrobial activity of PEM-2 for potential clinical applications further, we determined the solution structure of PEM-2 bound to membrane-mimetic dodecylphosphocholine (DPC) micelles by two-dimensional NMR methods. The DPC micelle-bound structure of PEM-2 adopts an α-helical conformation and the positively charged residues are clustered together to form a hydrophilic patch. The surface electrostatic potential map indicates that two of the three tryptophan residues are packed against the peptide backbone and form a hydrophobic face with Leu7, Ala9, and Leu10. A variety of biophysical and biochemical experiments, including circular dichroism, fluorescence spectroscopy, and microcalorimetry, were used to show that PEM-2 interacted with negatively charged phospholipid vesicles and efficiently induced dye release from these vesicles, suggesting that the antimicrobial activity of PEM-2 could be due to interactions with bacterial membranes. Potent analogues of PEM-2 with enhanced antimicrobial and less pronounced hemolytic activities were designed with the aid of these structural studies.

Identification of a heparin binding peptide from the Japanese encephalitis virus envelope protein.

The flavivirus envelope protein is the dominant antigen in eliciting neutralizing antibodies and plays an important role in inducing immunologic responses in the infected host. It has been shown that highly sulfated forms of heparin sulfate can bind to the envelope protein and are involved in flavivirus infection. Among the three structural domains, domain III is the major antigenic domain of the envelope protein. We have prepared an extended form of the JEV domain III protein with residues ranging from 261 to 402 and determined its heparin binding sites. Based on NMR, fluorescence spectroscopy, and site-directed mutagenesis studies, we have identified that only the N-terminal region (residues 279-293) and some spatially adjacent residues of JEV domain III are involved in heparin binding. Moreover, a synthetic peptide corresponding to this region also demonstrates strong affinity to heparin. Our results provide a basis for further understanding the interactions of flaviviruses and glycosaminoglycans on the host cell surfaces.

A new protocol for high-yield purification of recombinant human CXCL8((3-72))K11R/G31P expressed in Escherichia coli.

The ELR-CXC chemokines are important to neutrophil inflammation in many acute and chronic diseases. Among them, CXCL8 (interleukin-8, IL-8), binds to both the CXCR1 and CXCR2 receptors with high affinity and the expression levels of CXCL8 are elevated in many inflammatory diseases. Recently, an analogue of human CXCL8, CXCL8((3-72))K11R/G31P (hG31P) has been developed. It has been demonstrated that hG31P is a high affinity antagonist for both CXCR1 and CXCR2. To obtain large quantities of hG31P, we have successfully constructed and expressed hG31P in Escherichia coli. Moreover, we have developed a new protocol for high-yield purification of hG31P and for the removal of lipopolysaccharide (LPS, endotoxin) associated with hG31P due to the expression in E. coli. The purity of hG31P is more than 95% and the final yield is 9.7mg hG31P per gram of cell paste. The purified hG31P was tested by various biological assays. In addition, the structural properties of hG31P were studied by circular dichroism (CD), ultracentrifuge, isothermal titration calorimetry (ITC), and nuclear magnetic resonance (NMR) spectroscopy. Our results indicate that this purification protocol is very simple and easy to amplify at a large scale. The results of this study will provide an effective route to produce enough hG31P for future clinical studies.