Spectroscopic characterization of supramolecular chiral porphyrin homoassociates at the air-water interface.

The water-soluble 4-sulfonatophenyl meso-substituted porphyrin (TPPS) dye exhibits a transformation to a chiral self-aggregate from the non-aggregated species (diprotonated H4TPPS(2-)) at low concentration (no more than 1 × 10(-5) M). Immobilization of supramolecular chiral porphyrin homoassociates was mediated by the electrostatic interaction between the anionic TPPS molecule and cationic surfactant monolayer at the air-water interface. With the immobilization, a reversible transformation from monomeric TPPS to J-aggregate (M↔J) could be changed into an irreversible (M→J), which is desirable for stabilization of aggregation structure for a long period.

A new method for separating configurational and constitutional chiralities using diffuse reflectance circular dichroism (DRCD).

Solid-state chiral chemistry has attracted significant scientific interest because of its application in the chiral-selective production, chiral recognition, resolution, and detection of enantiomers of a chiral compound. Combining a novel diffuse reflectance circular dichroism (DRCD) technique with powder X-ray crystallographic analysis, we investigated the origin of chiral properties from the molecular and supramolecular chiralities and the possibility of separating independent CD signals from the superimposed CD signal resulting from different chiral origins.

Parasporin-1, a novel cytotoxic protein from Bacillus thuringiensis, induces Ca2+ influx and a sustained elevation of the cytoplasmic Ca2+ concentration in toxin-sensitive cells.

Parasporin-1 is a novel non-insecticidal inclusion protein from Bacillus thuringiensis that is cytotoxic to specific mammalian cells. In this study, we investigated the effects of parasporin-1 on toxin-sensitive cell lines to elucidate the cytotoxic mechanism of parasporin-1. Parasporin-1 is not a membrane pore-forming toxin as evidenced by measurements of lactate dehydrogenase release, propidium iodide penetration, and membrane potential in parasporin-1-treated cells.

Parasporin-1, a novel cytotoxic protein to human cells from non-insecticidal parasporal inclusions of Bacillus thuringiensis.

Pro-parasporin-1 is a parasporal inclusion protein of the non-insecticidal Bacillus thuringiensis strain A1190. Cytotoxic fragments, named parasporin-1, were generated from pro-parasporin-1 by trypsin digestion. Parasporin-1 was purified by a combination of chromatography procedures based on the cytotoxic activity to HeLa cells.