The electronic and spin states of a series of Co-Fe Prussian blue analogues containing Na(+) ion in the lattice, Na(x)()Co(y)()Fe(CN)(6) x zH(2)O, strongly depended on the atomic composition ratio of Co to Fe (Co/Fe) and temperature. Compounds of Co/Fe = 1.5 and 1.15 consisted mostly of the Fe(III)(t(2g)(5)e(g)(0), LS, S = 1/2)-CN-Co(II)(t(2g)(5)e(g)(2), HS, S = 3/2) site and the Fe(II)(t(2g)(6)e(g)(0), LS, S = 0)-CN-Co(III)(t(2g)(6)e(g)(0), LS, S = 0) site, respectively, over the entire temperature region from 5 to 350 K. Conversely, compounds of Co/Fe = 1.37, 1.32, and 1.26 showed a change in their electronic and spin states depending on the temperature. These compounds consisted mainly of the Fe(III)-CN-Co(II) site (HT phase) around room temperature but turned to the state consisting mainly of the Fe(II)-CN-Co(III) site (LT phase) at low temperatures. This charge-transfer-induced spin transition (CTIST) phenomenon occurred reversibly with a large thermal hysteresis of about 40 K. The CTIST temperature (T(1/2) = (T(1/2) descending + T(1/2) ascending)/2) increased from 200 to 280 K with decreasing Co/Fe from 1.37 to 1.26. Furthermore, by light illumination at 5 K, the LT phase of compounds of Co/Fe = 1.37, 1.32, and 1.26 was converted to the HT phase, and the relaxation temperature from this photoproduced HT phase also strongly depended on the Co/Fe ratio; 145 K for Co/Fe = 1.37, 125 K for Co/Fe = 1.32, and 110 K for Co/Fe = 1.26. All these phenomena are explained by a simple model using potential energy curves of the LT and HT phases. The energy difference of two phases is determined by the ligand field strength around Co(II) ions, which can be controlled by Co/Fe.
A novel series of 2-O-alkylascorbic acids (5a-u) was synthesized, and their scavenging activities against active oxygen species as well as their suppressive effects on the arrhythmias in rat heart ischemia-reperfusion models were evaluated. Some 2-O-alkylascorbic acids (5e-1) exhibited potent inhibiting activities against lipid peroxidation in rat brain homogenates and in alleviating effects in the ischemia-reperfusion models. Studies on the structure-activity relationship demonstrated that a free 3-enolic hydroxyl group and the longer alkyl chains substituted on the 2-hydroxyl group of ascorbic acid were beneficial for the biological and pharmacological activities. 2-O-Octadecylascorbic acid (5k, CV-3611), one of the most potent and promising compounds, markedly inhibited lipid peroxidation (IC50 = 4.3 X 10(-6) M) and alleviated myocardial lesions induced by ischemia-reperfusion at an oral dose of 1 mg/kg in rats.
Pathophysiological roles of endogenous endothelin have been studied from the viewpoint of its contribution to the extension of myocardial infarct size. A monoclonal antibody against endothelin 1 (AwETN40) suppressed changes induced by endothelin 1 and endothelin 2 but did not modify those by endothelin 3 in vivo or in vitro. Effects of AwETN40 on myocardial infarct size were investigated. Coronary ligation (1 hour) and reperfusion (24 hours) in rats caused infarction in 35% of the left ventricle. Repetitive or single administration of AwETN40 reduced the infarct size; an intravenous injection of 22.5 mg/kg of the antibody 5 minutes after coronary occlusion or 5 minutes before reperfusion reduced the size by 38% or 31% of the control, respectively. Plasma and tissue endothelin 1 and plasma big endothelin 1 in rats were measured at various stages after occlusion. Plasma endothelin 1 showed a fourfold increase 10 minutes after reperfusion (from 1.02 to 3.96 pg/ml) and had returned to the control value after 8 hours. Plasma big endothelin 1 showed changes similar to those of plasma endothelin 1. No significant changes in plasma endothelin 2 and endothelin 3 were observed. Cardiac tissue contained seven times as much endothelin 1 as the control value 1 hour after reperfusion (4.59 versus 33.1 pg/g tissue), and a high concentration (13.2 pg/g tissue) was maintained even after 48 hours. We concluded that an increase in endogenous endothelin 1 plays an important role in the extension of myocardial infarct size.
Real-time imaging of single-molecule fluorescence with a zero-mode waveguide (ZMW) was achieved. With modification of the ZMW geometry, the signal-to-background ratio is twice that obtainable with a conventional ZMW. The improved signal-to-background ratio makes it possible to visualize individual binding-release events between chaperonin GroEL and cochaperonin GroES at a concentration of 5 microM. Two rate constants representing two-timer kinetics in the release of GroES from GroEL were measured with the ZMW, and the measurements agreed well with those made with a total internal reflection fluorescence microscopy. These results indicate that the novel ZMW makes feasible the direct observation of protein-protein interaction at an intracellular concentration in real time.
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