Production of multicharged ions and behavior of microwave modes in an electron cyclotron resonance ion source directly excited in a circular cavity resonator Rev. Sci. Instrum. 77, 03A336 (2006); 10.1063/1.2163330 All-metamaterial-based subwavelength cavities ( λ ∕ 60 ) for ultrathin directive antennas Appl. Phys. Lett. 88, 084103 (2006); 10.1063/1.2172740Resonantly coupled surface plasmon polaritons in the grooves of very deep highly blazed zero-order metallic gratings at microwave frequencies

Alginate/chitosan/alginate (ACA) hydrogel microcapsules were modified with methoxy poly(ethylene glycol) (MPEG) to improve protein repellency and biocompatibility. Increased MPEG surface graft density (n(S)) on hydrogel microcapsules was achieved by controlling the grafting parameters including the buffer layer substrate, membrane thickness, and grafting method. X-ray photoelectron spectroscopy (XPS) model was employed to quantitatively analyze n(S) on this three-dimensional (3D) hydrogel network structure. Our results indicated that neutralizing with alginate, increasing membrane thickness, and in situ covalent grafting could increase n(S) effectively. ACAC(PEG) was more promising than ACC(PEG) in protein repellency because alginate supplied more -COO(-) negative binding sites and prevented MPEG from diffusing. The n(S) increased with membrane thickness, showing better protein repellency. Moreover, the in situ covalent grafting provided an effective way to enhance n(S), and 1.00 ± 0.03 chains/nm(2) was achieved, exhibiting almost complete immunity to protein adsorption. This antifouling hydrogel biomaterial is expected to be useful in transplantation in vivo.

We report the influence of surface morphology and charge of alginate/chitosan (ACA) microcapsules on both the amount of adsorbed protein and its secondary structural changes during adsorption. Variations in surface morphology and charge were controlled by varying alginate molecular weight and chitosan concentration. Plasma fibrinogen (Fgn) was chosen to model this adsorption to foreign surfaces. The surface of ACA microcapsules exhibited a granular structure after incubating calcium alginate beads with chitosan solution to form membranes. The surface roughness of ACA microcapsule membranes decreased with decreasing alginate molecular weight and chitosan concentration. Zeta potential measurements showed that there was a net negative charge on the surface of ACA microcapsules which decreased with decreasing alginate molecular weight and chitosan concentration. The increase in both surface roughness and zeta potential resulted in an increase in the amount of Fgn adsorbed. Moreover, the higher the zeta potential was, the stronger the protein-surface interaction between fibrinogen and ACA microcapsules was. More protein molecules adsorbed spread and had a greater conformational change on rougher surfaces for more surfaces being available for protein to attach.

Aeromonas caviae CB101 secretes four chitinases (around 92, 82, 70, and 55 kDa) into the culture supernatant. A chitinase gene chi1 (92 kDa) was previously studied. To identify the genes encoding the remaining three chitinases, a cosmid library of CB101 was constructed to screen for putative chitinase genes. Nine cosmid clones were shown to contain a chitinase gene on chitin plates. Surprisingly, all the positive clones contained chi1. In parallel, we purified the 55-kDa chitinase (Chi55) from the CB101 culture supernatant by continuous DEAE-Sepharose and Mono-Q anion exchange chromatography. The N-terminal amino acid sequence of the purified chitinase exactly matched the N-terminal sequence of mature Chi1, indicating that the purified chitinase (Chi55) is a truncated form of Chi1. The N- and C-terminal domains of chi1 were cloned, expressed, and purified, separately. Western blots using anti-sera to the N- and C-terminal domains of chi1 on the chitinases of CB101 showed that the four chitinases in the culture supernatant are either chi1 or C-terminal truncations of Chi1. In addition, the CB101 chi1 null mutant showed no chitinolytic activity, while CB101 chi1 null mutant complemented by pUC19chi1 containing chi1 showed all four chitinases in gel activity assay. These data indicated that all four chitinases secreted by CB101 in the culture supernatant are the product of one chitinase gene chi1.