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1.  Efficient adsorption and photocatalytic degradation of Congo red onto hydrothermally synthesized NiS nanoparticles 
NiS nanoparticles (NiS NPs) have been hydrothermally prepared and characterized by the methods of X-ray diffraction, scanning electronic microscope, X-ray photoelectron spectroscopy, UV–Vis diffuse reflectance spectra, photoluminescence, and thermogravimetric analysis. NiS NPs exhibit fast adsorption in the removal of Congo red (CR) in aqueous solution, in which the pseudo-second-order model was the best to describe the adsorption kinetics, and the intraparticle diffusion was not only the rate-limiting step. The NiS NPs also exhibit efficient photocatalytic activity in the degradation of CR under visible-light irradiation, in which the 30 mg/L CR was almost completely degraded after illumination during 210 min. The •OH radicals in the process of photocatalytic degradation were observed by fluorescence technique.
doi:10.1007/s11051-013-1475-y
PMCID: PMC3601262  PMID: 23519156
NiS nanoparticles; Adsorption; Photocatalytic degradation; Congo red; Mechanism
2.  The X Protein of Hepatitis B Virus Inhibits Apoptosis in Hepatoma Cells through Enhancing the Methionine Adenosyltransferase 2A Gene Expression and Reducing S-Adenosylmethionine Production* 
The Journal of Biological Chemistry  2011;286(19):17168-17180.
The X protein (HBx) of hepatitis B virus (HBV) is involved in the development of hepatocellular carcinoma (HCC), and methionine adenosyltransferase 2A (MAT2A) promotes the growth of liver cancer cells through altering S-adenosylmethionine homeostasis. Thus, we speculated that a link between HBx and MAT2A may contribute to HCC development. In this study, the effects of HBx on MAT2A expression and cell apoptosis were investigated, and the molecular mechanism by which HBx and MAT2A regulate tumorigenesis was evaluated. Results from immunohistochemistry analyses of 37 pairs of HBV-associated liver cancer tissues/corresponding peritumor tissues showed that HBx and MAT2A are highly expressed in most liver tumor tissues. Our in vitro results revealed that HBx activates MAT2A expression in a dose-dependent manner in hepatoma cells, and such regulation requires the cis-regulatory elements NF-κB and CREB on the MAT2A gene promoter. Electrophoretic mobility shift assay (EMSA) and chromatin immunoprecipitation (ChIP) further demonstrated that HBx facilitates the binding of NF-κB and CREB to MAT2A gene promoter. In addition, overexpression of HBx or MAT2A inhibits cell apoptosis, whereas knockdown of MAT2A expression stimulates apoptosis in hepatoma cells. Furthermore, we demonstrated that HBx reduces MAT1A expression and AdoMet production but enhances MAT2β expression. Thus, we proposed that HBx activates MAT2A expression through NF-κB and CREB signaling pathways to reduce AdoMet production, inhibit hepatoma cell apoptosis, and perhaps enhance HCC development. These findings should provide new insights into our understanding how the molecular mechanisms underline the effects of HBV infection on the production of MAT2A and the development of HCC.
doi:10.1074/jbc.M110.167783
PMCID: PMC3089560  PMID: 21247894
Apoptosis; Cancer Tumor Promoter; Chromatin Immunoprecipitation (ChiP); CREB; DNA-Protein Interaction; DNA Viruses; Gene Regulation; Hepatitis Virus; Oncogene; S-Adenosylmethionine (AdoMet)
3.  Antioxidant and Antiproliferative Activities of Heated Sterilized Pepsin Hydrolysate Derived from Half-Fin Anchovy (Setipinna taty) 
Marine Drugs  2011;9(6):1142-1156.
In this paper we studied the antioxidant and antiproliferative activities of the heated pepsin hydrolysate from a marine fish half-fin anchovy (HAHp-H). Furthermore, we compared the chemical profiles including the amino acid composition, the browning intensity, the IR and UV-visible spectra, and the molecular weight distribution between the half-fin anchovy pepsin hydrolysate (HAHp) and HAHp-H. Results showed that heat sterilization on HAHp improved the 1,1-diphenyl-2-picryl-hydrazil (DPPH) radical-scavenging activity and reducing power. In addition, the antiproliferative activities were all increased for HAHp-H on DU-145 human prostate cancer cell line, 1299 human lung cancer cell line and 109 human esophagus cancer cell line. The contents of free amino acid and reducing sugar of HAHp-H were decreased (P < 0.05). However, hydrophobic amino acid residues and the browning intensity of HAHp-H were increased. FT-IR spectroscopy indicated that amide I and amide III bands of HAHp-H were slightly modified, whereas band intensity of amide II was reduced dramatically. Thermal sterilization resulted in the increased fractions of HAHp-H with molecular weight of 3000–5000 Da and below 500 Da. The enhanced antioxidant and antiproliferative activities of HAHp-H might be attributed to the Maillard reaction.
doi:10.3390/md9061142
PMCID: PMC3131565  PMID: 21747752
half-fin anchovy pepsin hydrolysate; heated sterilization; antioxidant activity; antiproliferative activity; chemical profile
4.  Adsorption of Pb(II) and Cd(II) by Squid Ommastrephes bartrami Melanin 
The adsorption of Cd(II) and Pb(II) by squid melanin was investigated. At a metal ion concentration of 2 mM/L, the biosorption efficiency of melanin reached 95% for Cd(II) and Pb(II). The maximum content of bound Cd(II) and Pb(II) was 0.93 mM/g and 0.65 mM/g, respectively. Temperature had no obvious effect on the adsorption of the metals, and in a pH range of 4.0–7.0, the adsorption yield was high and stable. Macrosalts such as NaCl, MgCl2, and CaCl2 had no obvious effect on the binding of Pb(II) but greatly diminished the adsorption of Cd(II), which indicated that different functional groups in squid melanin are responsible for their adsorption. IR analysis of metal ion-enriched squid melanin demonstrated that the possible functional groups responsible for metal binding were phenolic hydroxyl (OH), carboxyl (COOH), and amine groups (NH). This study reports a new material for the removal of heavy metals from low-strength wastewater.
doi:10.1155/2009/901563
PMCID: PMC2817865  PMID: 20148082

Results 1-4 (4)