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2 poly(u) . 1 adenosine complex formation was studied by spin-technique in the temperature range from 7 to 25 degrees C. It is shown that adenosine binding induces the conformational transition of poly(u) structure from flexible coil into rigid helix. The contribution of hydrogen bonding and stacking of adenosine to the total change of enthalpy and entropy upon complex formation was estimated.
The flow-sensitive alternating inversion recovery (FAIR) and the first-pass dynamic contrast-enhanced MR imaging (CE-MRI) techniques have both been shown to be effective in the assessment of human pulmonary perfusion. However, no comprehensive comparison of the measurements by these two methods has been reported. In this study, healthy adults were recruited, with FAIR and CE-MRI performed for an estimation of the relative pulmonary blood flow (rPBF). Regions of interest were encircled from the right and left lungs, with right-to-left rPBF ratios calculated. Results indicated that, on posterior coronal slices, the rPBF ratios obtained with the FAIR technique agreed well with CE-MRI measurements (mean difference = -0.02, intraclass correlation coefficient RI = 0.78, 95% confidence interval = [0.67, 0.86]). On middle coronal slices, however, FAIR showed a substantially lower rPBF by up to 43% in the right lung compared with CE-MRI (mean difference = -0.38, RI = 0.34, 95% confidence interval = [-0.09, 0.68]). The location-dependent discrepancy between measurements by FAIR and CE-MRI methods is attributed to tracer saturation effects of arterial inflow when the middle coronal slice contains the in-plane-oriented right pulmonary artery, whereas the left lung rPBF is less affected due to oblique orientation of the left pulmonary artery. Intrasequence comparison on additional subjects using FAIR at different slice orientations supported the above hypothesis. It is concluded that FAIR imaging for pulmonary perfusion in the coronal plane provides equivalent rPBF information with CE-MRI only in the absence of tracer saturation effects; hence, FAIR should be carefully exercised to avoid misleading interpretations.
The electron spin resonance (EPR) spectrum of erythrocyte membranes labeled with 2,2,6,6-tetra-methyl-4-maleimido-piperidin-1-oxyl (MAL-6) indicates both weakly and strongly immobilized labeling sites. Changes in the ratio of the membrane's low field spectral peaks (W/S) have often been used to monitor drug-erythrocyte interactions. We have investigated a number of experimental factors that may influence this ratio even in the absence of drug. Instrumental settings on the EPR spectrometer had no obvious effect. As the weight ratio of label/protein decreased, the W/S ratio increased. Similarly an increase in labeling time and temperature lead to an increase in the ratio. The ratio also increased with time after labeling; this change was most marked in samples kept at 37 degrees C, but was insignificant in samples kept at 4 degrees C. Increasing the viscosity of the sample with low-molecular-weight substances such as sucrose or glycerol, but not with those with high molecular weight such as dextran and PVP, caused a reduction in the ratio. Increasing the pH and changing the buffer concentrations also lead to a small increase in W/S. These results suggest that it is very important that all of these factors be kept constant and at some optimal value if reliable and consistent results are to be obtained using this method to monitor drug-erythrocyte interactions.
Using electron spin resonance stop-flow technique, the transverse motion (flip-flop) of 3-([alpha-carboxy-4-(4-hydroxy-3-iodophenoxy)-3,5- diiodophenethyl]carbamoyl)-2,2,5,5-tetramethyl-3-pyrrolin (T3-SL) in dipalmitoyl L-alpha-phosphosphatidylcholine (DPPC) membranes was evaluated. At 22 degrees C, the electron spin resonance spectra of T3-SL in DPPC vesicles were compared before and after the addition of sodium ascorbate, a membrane impermeable reducing agent. The addition of ascorbate reduces the signal amplitude by 67% in 3 min but yields no further reduction for at least 60 min. These results indicate that T3-SL does not flip-flop at any appreciable rate in the membranes. This finding suggests that once partitioned into the membrane, T3 remains in the outer half of the lipid bilayer, thus reducing the possibility that T3 enters the cell by passive diffusion.
Dioctadecyldimethylammonium bromide (DODAB) dispersions obtained by simply mixing the amphiphile in water, and by bath-sonication, were investigated by electron spin resonance (ESR) of stearic acids and their methyl ester derivatives, labeled at the 5th and 16th carbons of the acyl chain. The ESR spectra indicate that the non-sonicated dispersions are formed mainly by one population of DODAB vesicles, either in the gel (T T(m)) state. Around T(m) there is a co-existence of the two phases, with a thermal hysteresis of about 3.2 degrees C. In sonicated DODAB dispersions, spin labels indicate two different environments even for temperatures far below T(m): one similar to that obtained with non-sonicated samples, a gel phase, and another one in the liquid-crystalline state. The fluid phase domain present below T(m) could correspond to either the periphery of bilayer fragments, reported to be present in sonicated DODAB dispersions, or to high curvature vesicles.
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Imaging of a tumor with ESR was tried using two different types of spin probes, a low molecular weight spin probe, CPROXYL, and a polymer spin probe, TEMPO-DX. Spin probes were administered to a mouse bearing a solid tumor that was a transplanted Ehrlich's ascites carcinoma in the back, using two methods, conventional intraperitoneal injection and continuous intravenous injection with a micro-feeder. First, the accumulation of the probe was examined by X-band ESR. CPROXYL, which was administered to a mouse intraperitoneally, was exclusively retained in urine, showing that it was rapidly excreted into the bladder, while TEMPO-DX was absorbed from the peritoneal cavity with difficulty to the vessel. Using continuous intravenous injection, CPROXYL was also rapidly excreted, but it was confirmed that TEMPO-DX concentrated in tumor tissue because it has a long half-life in vivo. In addition, measurement of ESR imaging was done to measure the distribution of spin probes with continuous intravenous injection. The strongest spot of CPROXYL was observed on ESR images, showing the accumulation at the bladder, while the spot of TEMPO-DX was observed in the solid tumor of the back of the mouse. These results suggest that TEMPO-DX could stay much longer than a low molecular weight spin probe in vivo and concentrate at the tumor. TEMPO-DX may be useful for developing specific ESR imaging agents for tumor.
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