Kyung Soo Hahm

Antioxidative constituents fromBuddleia officinalis

Four flavonoids (1-4), a phenylethyl glycoside (5), and a phenylpropanoid glycoside (6) were isolated from the flowers of Buddleia officinalis (Loganiaceae). Their structures were determined by chemical and spectral analysis. Among the isolated compounds, luteolin (1) and acteoside (6) exhibited the most potent antioxidative activity on the NBT superoxide scavenging assay. In addition, compounds 1-6 revealed weak antifungal activity, and no hemolytic activity.Four flavonoids (1–4), a phenylethyl glycoside (5), and a phenylpropanoid glycoside (6) were isolated from the flowers ofBuddleia officinalis (Loganiaceae). Their structures were determined by chemical and spectral analysis. Among the isolated compounds, luteolin (1) and acteoside (6) exhibited the most potent antioxidative activity on the NBT superoxide scavenging assay. In addition, compounds1–6 revealed weak antifungal activity, and no hemolytic activity.

A hybrid peptide derived from cecropin-A and magainin-2 inhibits osteoclast differentiation

The adult skeleton is in a dynamic state, being continually broken down and reformed by the coordinated actions of osteoclasts and osteoblasts. Increased osteoclast activity may contribute to the development of osteoporosis. Therefore, the intervention of osteoclast-mediated bone resorption is considered as an effective therapeutic approach in the treatment of osteoporosis. In the course of searching for agents that inhibit osteoclast differentiation and activation, we found that a novel hybrid peptide P1 derived from cecropin-A and magainin-2 reduced osteoclast differentiation in various osteoclast culture systems. As this peptide had no cytotoxicity on various cultures of primary cells and established cell lines, its inhibitory effect on osteoclastogenesis was not due to general cytotoxicity. The effects of P1 on osteoclasts appear to be mediated through the inhibition of NF-kappaB and JNK activation induced by the osteoclastogenic cytokine, receptor activator of NF-kappaB ligand (RANKL). These results provide an evidence for the potential usefulness of P1 for the treatment of bone-resorbing diseases.

Mass production of methane from food wastes with concomitant wastewater treatment.

We developed a process for production of methane at a pilot scale. This process consists of three stages. The first stage is a semianaerobic hydrolysis/acidogenic step in which organic wastes are converted to various sugars, amino acids, and volatile fatty acids (VFAs). Operation temperature and pH were 45 degrees C, and 5.0-5.5, respectively. Hydraulic retention time (HRT) was 2 d. To remove the putrid odor and to enhance the hydrolysis of organic wastes, a mixture of bacteria isolated from landfill soil was inoculated into the reactor. Total chemical oxygen demand (tCOD) and biological oxygen demand (BOD) were 36,000 mg/L and 40,000 mg/L, respectively. The second stage was an anaerobic acidogenic process, which can produce large amount of VFAs including acetate, propionate, butyrate, valerate, and caproate. Operation temperature and pH were 35 degrees C, and 5.0-5.5, respectively. HRT was 2 d. The third stage was a strictly anaerobic methane fermentation step producing methane and carbon dioxide from VFAs. The working volume of upflow anaerobic sludge blanket (UASB) type reactor was 1200 L, and operation temperature and pH were 41 degrees C, and 7.7-7.9, respectively. HRT was 12 d. Seventy two percent of methane at maximum was generated and the yield was 0.45-0.50 m3/kgVS of food wastes. Through the process, 88% of tCOD and 95% of BOD were removed. The wastewater was treated with the biological aerobic and anaerobic filters immobilized with heterotrophic and autotrophic nitrifying and denitrifying bacteria. Ninety percent of total nitrogen (T-N) was removed by this treatment. The residual T-N and total phosphorous (T-P) were removed by the algal periphyton treatment system. The final concentrations of nitrogen and phosphorous in the drain water were 53 and 7 mg/L, respectively.

Purification and characterization of two forms of methanol dehydrogenases from a marine methylotroph.

Two methanol dehydrogenases (MDHs), MDH1 and MDH2, were purified from a marine methylotroph, Methylophaga sp. strain 1. Both enzymes had very similar properties, including the same native molecular weight, sizes of subunits and substrate specificity. The N‐terminal amino acid sequence of the α‐subunit of MDH2 differed from that of MDH1 by having a histidine residue at a highly conserved glutamate position, but both sequences showed approximately 50% homology to the α‐subunits of other MDHs. MDH1 had higher specific activity than MDH2 with respect to methanol and ethanol as a substrate. The two enzymes did not appear to be isoforms but that either MDH1 or MDH2 could be a mutant arising from spontaneous mutation.

Mechanism of antibacterial action of a synthetic peptide with an Ala-peptoid residue based on the scorpion-derived antimicrobial peptide IsCT

A novel bacterial cell-selective antimicrobial peptide, IsCT-P (ILKKIWKPIKKLF-NH2), was designed based on the scorpion-derived α-helical antimicrobial peptide, IsCT. Here, we investigated the effect of substituting Pro8 of IsCT-P with the Ala-peptoid residue (N-methylglycine) on the peptide’s structure and mechanism of action. Circular dichroism analysis revealed that the modified peptide, IsCT-a, has a much lower α-helicity than IsCT-P in membrane mimicking conditions, suggesting the peptoid residue provides much more structural flexibility than the proline residue. IsCT-a was also much less effective than IsCT-P at causing leakage of fluorescent dye entrapped within negatively charged vesicles and at dissipating the membrane potential of Staphylococcus aureus. Collectively, our results suggest that the antibacterial action of IsCT-a is due to the inhibition of intracellular targets rather than the disruption and depolarization of bacterial cell membranes.