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1.  Stability and cytotoxicity of angiotensin-I-converting enzyme inhibitory peptides derived from bovine casein*  
This study investigated the effect of heat treatment combined with acid and alkali on the angiotensin-I-converting enzyme (ACE) inhibitory activity of peptides derived from bovine casein. The free amino group content, color, and cytotoxicity of the peptides were measured under different conditions. When heated at 100 °C in the pH range from 9.0 to 12.0, ACE inhibitory activity was reduced and the appearance of the peptides was significantly darkened. After thermal treatment in the presence of acid and alkali, the free amino group content of ACE inhibitory peptides decreased markedly. High temperature and prolonged heating also resulted in the loss of ACE inhibitory activity, the loss of free amino groups, and the darker coloration of bovine casein-derived peptides. However, ACE inhibitory peptides, within a concentration range of from 0.01 to 0.2 mg/ml, showed no cytotoxicity to Caco-2 and ECV-304 cell lines after heat treatment. This indicated that high temperature and alkaline heat treatment impaired the stability of bovine casein-derived ACE inhibitory peptides.
PMCID: PMC3924390  PMID: 24510707
Angiotensin-I-converting enzyme inhibitory peptide; Heat treatment; Stability; Cytotoxicity
2.  Controllable effects of quantum fluctuations on spin free-induction decay at room temperature 
Scientific Reports  2012;2:432.
Fluctuations of local fields cause decoherence of quantum objects. Usually at high temperatures, thermal noises are much stronger than quantum fluctuations unless the thermal effects are suppressed by certain techniques such as spin echo. Here we report the discovery of strong quantum-fluctuation effects of nuclear spin baths on free-induction decay of single electron spins in solids at room temperature. We find that the competition between the quantum and thermal fluctuations is controllable by an external magnetic field. These findings are based on Ramsey interference measurement of single nitrogen-vacancy center spins in diamond and numerical simulation of the decoherence, which are in excellent agreement.
PMCID: PMC3362804  PMID: 22666535
3.  Poly[[bis­(2,2-bipyridine)­bis­[μ6-5-(carboxyl­atometh­oxy)benzene-1,3-dicarboxyl­ato]trimanganese(II)] monohydrate] 
The title compound, {[Mn3(C10H5O7)2(C10H8N2)2]·H2O}n, was synthesized under hydro­thermal conditions. Six carboxyl­ate groups of six 5-(carboxyl­atometh­oxy)benzene-1,3-dicarboxyl­ate anions (OABDC3−) join three MnII ions into a trinuclear centrosymmetric [Mn3(μ2-COO)6] unit with one Mn site situated on a centre of inversion. The latter MnII ion exhibits a distorted MnO6 coordination, whereas the other MnII ion has a trigonal–bipyramidal MnN2O3 coordination environment resulting from three carboxylate O atoms and the two N atoms of the bipyridine ligand. Adjacent units are linked to each other by OABDC3− ligands into a layer parallel to (010). Within the layer, O—H⋯O hydrogen-bonding inter­actions involving the uncoordinated and half-occupied water mol­ecule and the free carboxyl­ate O atoms are observed. The layers stack along [010], constructing a three-dimensional structure through π–π inter­actions between adjacent pyridine rings, with a centroid–centroid distance of 3.473 (5) Å.
PMCID: PMC3051434  PMID: 21522911
4.  Dopamine and Ethanol Cause Translocation of εPKC Associated with εRACK: Cross-talk Between PKA and PKC Signaling Pathways 
Molecular pharmacology  2008;73(4):1105-1112.
Previously we found that neural responses to ethanol and the dopamine D2 receptor (D2) agonist NPA involve both epsilon protein kinase C (εPKC) and cAMP-dependent protein kinase A (PKA). However, little is known about the mechanism underlying ethanol- and D2-mediated activation of εPKC and the relationship to PKA activation. In the present study, we used a new εPKC antibody, 14E6, that selectively recognizes active εPKC when not bound to its anchoring protein εRACK (receptor for activated C-kinase), and PKC isozyme-selective inhibitors and activators, to measure PKC translocation and catalytic activity. We show here that ethanol and NPA activated εPKC and also induced translocation of both εPKC and its anchoring protein, εRACK to a new cytosolic site. The selective εPKC agonist, pseudo-εRACK, activated εPKC but did not cause translocation of the εPKC/εRACK complex to the cytosol. These data suggest a step-wise activation and translocation of εPKC following NPA or ethanol treatment where εPKC first translocates and binds to its RACK and subsequently the εPKC/εRACK complex translocates to a new subcellular site. Direct activation of PKA by Sp-cAMPS, PGE1 or the adenosine A2A receptor is sufficient to cause εPKC translocation to the cytosolic compartment in a process that is dependent on PLC activation and requires PKA activity. These data demonstrate a novel cross-talk mechanism between εPKC and PKA signaling systems. PKA and PKC signaling have been implicated in alcohol rewarding properties in the mesolimbic dopamine system. Cross-talk between PKA and PKC may underlie some of the behaviors associated with alcoholism.
PMCID: PMC2692587  PMID: 18202306

Results 1-4 (4)