Gas-liquid Chromatographic Separation of Amine Enantiomers as Diastereoisomeric Chrysanthemoylamide Derivatives

An immobilized chloroplast film, prepared by immobilizing spinach chloroplasts in 2 wt% agar gel, was attached to a SnO₂ optically transparent electrode to obtain the immobilized chloroplast film electrode. The immobilized chloroplast film electrode worked as a photoanode under illumination in the presence of methyl viologen, which was an electron carrier from chloroplasts to the SnO₂ optically transparent electrode. Water photolysis for producing hydrogen by a photoelectrochemical cell using the immobilized chloroplasts film electrode was successfully achieved. A smooth platinum electrode was used as a cathode to produce hydrogen. The pH and temperature of the anolyte were kept at 7.8 and 25°C. Optimizations of the concentrations of methyl viologen and chlorophyll in the immobilized chloroplast film were studied. The optimum thickness for the immobilized chloroplast film was about 0.8 mm. The immobilized chloroplasts had higher storage stability than that of isolated chloroplasts and they retained more than 50% of the initial activities of photosystem I and photosystem II after 10 days when they were stored at 4°C in the dark. It was conceived from the relationship between the photocurrent and the photosystem I and II activities that the main cause for the decrease in the photocurrent was the photochemical inactivation of photosystem II.     

Evidence of colorectal cancer risk associated variant Lys25Ser in the proximity of human bone morphogenetic protein 2

Colorectal cancer (CRC) is the third most prevalent cancer and fourth leading cause of cancer-related deaths globally. It has been shown that the nsSNP variants play an important role in diseases, however it remained unclear how these variants are associated with the disease. Recently, several CRC risk associated SNPs have been discovered, however rs961253 (Lys25Arg at 20p12.3) located in the proximity of bone morphogenetic protein 2 (Bmp2) and fermitin family homolog 1 Fermt1 genes have been reported to be highly associated with the CRC risk. Here we provide evidence for the first time in silico biological functional and structural implications of non-synonymous (nsSNPs) CRC disease-associated variant Lys25Arg via molecular dynamic (MD) simulation. Protein structural analysis was performed with a particular variant allele (A/C, Lys25Arg) and compared with the predicted native protein structure. Our results showed that this nsSNP will cause changes in the protein structure and as a result is associated with the disease. In addition to the native and mutant 3D structures of CRC associated risk allele protein domain (CRAPD), they were also analyzed using solvent accessibility models for further protein stability confirmation. Taken together, this study confirmed that this variant has functional effect and structural impact on the CRAPD and may play an important role in CRC disease progression; hence it could be a reasonable approach for studying the effect of other deleterious variants in future studies.