Opioid antagonist peptides derived from kappa-casein

Opioid antagonists were sought in the fragments of kappa-casein which were obtained by chemical synthesis and enzymic digestion. A synthetic bovine kappa-casein peptide (35-41), Tyr-Pro-Ser-Tyr-Gly-Leu-Asn (casoxin A) showed opioid antagonist activity at 200 microM in the guinea pig ileum assay. A synthetic peptide Tyr-Pro-Tyr-Tyr (casoxin B) which is found in bovine and human kappa-casein, also showed opioid antagonist activity at 100 microM. Another opioid antagonist peptide (casoxin C) was isolated from tryptic digests of bovine kappa-casein by reverse-phase HPLC. The structure of the peptide was Tyr-Ile-Pro-Ile-Gln-Tyr-Val-Leu-Ser-Arg, which corresponded to kappa-casein (25-34). Casoxin C was active at 5 microM in the guinea pig ileum assay. Thus, bovine kappa-casein contains three potential opioid antagonist sequences.     

Mechanism for degradation of poly(sodium acrylate) by bacterial consortium no. L7-98

Poly(sodium acrylate) (PSA) can be degraded by consortia of several bacterial species. We investigated the degradation mechanism for PSA (average molecular weight, 2100) by consortium no. L7-98. PSA was used as the sole carbon source in a mineral salt medium. After cultivation, the PSA had a range of molecular weights, including low-molecular-weight compounds, which were purified by gel-permeation and reversed-phase column chromatography. One purified compound, B1, with the molecular weight of 200, had a carbonyl group next to the terminus, according to 1H and 13C nuclear magnetic resonance spectrometry and X-ray analysis of the crystal structure. Two categories of metabolites of PSA were detected in the culture by electrospray ionization mass spectrometry. Results of high-resolution mass spectrometry (HR-MS) suggested that one kind of compounds had a carbonyl group and that the other kind of compounds had an aldehyde group and a double bond. Compounds having the molecular weights of 200 and 272 were rapidly produced from an acrylic acid oligomer with the molecular weight of 258 by resting cells of the consortium. HR-MS showed that a methylene group at the terminal unit was oxidized to a carbonyl group and that the compound with the molecular weight of 200 was compound B1. From these results, we propose that the degradation pathway of PSA involves (i) oxidation of a methylene group to a carbonyl group next to the terminus, (ii) decarboxylation to form an aldehyde group and dehydrogenation to form a double bond between the terminal unit and the next unit, and (iii) oxidation of the aldehyde group to a carboxyl group followed by elimination of an acetic acid.     

A study of mesh deformation methods for magnetic field analysis

In this paper, we describe a study of mesh deformation methods for magnetic field analysis. We propose an efficient method that is a combination of two conventional mesh deformation methods. We numerically estimate the basic performance of the proposed method and conventional methods using three‐dimensional mesh models for magnetic field analysis. We highlight the advantages of the proposed method with respect to its robustness and computational cost. © 2011 Institute of Electrical Engineers of Japan. Published by John Wiley & Sons, Inc.     

Extractive solubilization, structural change, and functional conversion of cytochrome c in ionic liquids via crown ether complexation

This article reports on the extraction behavior of heme proteins from an aqueous phase into ionic liquids (ILs) with dicyclohexano-18-crown-6 (DCH18C6), and the structure-function relationship of cytochrome c (Cyt-c) dissolved in ILs. We have found that DCH18C6 enables transfer of Lys-rich proteins into ILs via supramolecular complexation. The hydrophobicity and functional groups of ILs have a great influence on protein partitioning, and a hydroxyl group-containing IL with DCH18C6 is capable of the quantitative partitioning of Cyt-c. On the other hand, protein transfer using conventional organic solvents is negligibly small. UV-visible, CD, and resonance Raman spectroscopic characterizations indicate that the sixth ligand Met 80 in the heme group of the Cyt-c-DCH18C6 complex in IL is replaced by other amino acid residues of the peptide chain and that a non-natural, six-coordinate, low-spin ferric heme structure is induced in IL. Solubilization of Cyt-c in IL causes the environmental change of the heme vicinity of Cyt-c, which triggers the functional conversion of Cyt-c from an electron-transfer protein to peroxidase. The Cyt-c-DCH18C6 complex in IL provides remarkably high peroxidase activity compared with native Cyt-c, because of enhancement of the affinity for H2O2.