小白鼠肌肉组织的NMR质子自旋交换分析

本文在Zimmerman-Brittin两相质子交换核磁共振弛豫模型基础上,分析了NMR弛豫实验中检测信号与各相表现和本征弛豫多数的关系,编写了自动化处理实验数据的计算机程序,这一技术可用于复相系统中不同成分的NMR表现和本征弛豫特性研究中,本文中的样品是选用健康新鲜的小白鼠肌肉,没加任何处理,用h-h,s-h,s-s脉冲序列,反转恢复法(π-τ-π/2)在强场下(0.92T)做T₁、T₂测定实验,分析结果表明本征弛豫参数T₁=1050ms,T₂=4500μs的成分是由肌肉中的"自由水"引起的,其质子相对含量为69%;本征弛豫参数T₁=530ms,T₂=26μs的成分是由肌肉中的"束附水"引起的,其质子相对含量为9%,本征弛豫多数T₁=530ms,T₂=1250μs的成分是由肌肉中的各种大分子和有机物引起的,其质子相对含量为9%,本征弛豫参数T₁=470ms,T₂=1250μs的成分由样品中的脂肪引起的,其质子相对含量为13%,在肌肉组织中的质子与水中质子之间有强烈的交换作用,其交换率k=1000s^-1.在脂肪中的质子与其它成分之间没有交换作用。     

超顺磁性氧化铁-胶束体系的制备和T2弛豫增强作用 

制备了在负离子型胶束十二烷基硫酸钠（SDS）、羧甲基纤维素钠（CMC），正离子型胶束十六烷基三甲基溴化铵（CTAB）和非离子型胶束Triton X-100、PEG-400中的氧 化铁粒子(SPIO)溶胶分散体系. 测定了这些SPIO胶束体系水质子的横向弛豫时间T₂, 并讨论了不同胶束性质对T₂的影响. 对PEG-400分散SPIO溶胶体系进行了动物急性毒性测试和活体T₂加权成像实验. 结果表明：该溶胶体系无明显急性毒性，且对大鼠肝区有显著的负增强.     

四卤化锡混合物中受扩散控制的卤原子交换动力学研究

以¹¹⁹Sn NMR 方法研究了四氯化锡和四溴化锡混合物（1∶1, 摩尔比）交换体系在不同条件下的动力学性质. 测定了在不同浓度的氘代氯仿溶液中5个交换组份的表观纵向弛豫时间（T¹）及5个组份相互间的交换速率常数（k）,结果表明交换速率常数与表观纵向弛豫速率成正比关系;同时,根据¹¹⁹Sn 1D NMR信号的线宽估测了有效横向弛豫时间（T^*₂）,并由T₁/T^*₂推断在所研究的体系中分子的运动属NMR慢运动极限. 从实验结果可推断在所研究的复杂交换体系中5个组份间的交换与分子自扩散运动有关,即化学交换与交换主体的扩散运动有必然的联系.     

分子间多量子相干横向弛豫时间(和自扩散系数)测量的参数优化和数据处理方法

针对测量横向弛豫时间T₂的CPMG脉冲序列和我们所设计的可同时测量高极化单组份单 峰核自旋体系n阶分子间多量子相干横向弛豫时间T_2,n和自扩散系数D_n的改进的CRAZED脉冲序列,分析了影响测量T₂、T_2,n（或D_n）的各种因素,并着重从技术方面讨论了准确测量T_2,n和D_n的实验参数优化和实验数据处理方法.     

癸基萘磺酸钠胶束中分子动态的质子核磁共振研究

在298、303和313 K下对浓度为0.82 和2.59 mmol/L的癸基萘磺酸钠的重水溶液中质子的自旋-自旋弛豫（T₂）时间进行了测量. 浓度为0.82 mmol/L 的溶液(临界胶束浓度CMC以下)中的所有质子的T₂值均随温度上升而增长，说明整个分子运动变的更自由. 然而，浓度在CMC以上(2.59 mmol/L)时，分子中一部分参与形成栅栏层的质子的T₂值却表现出相反的效应，它们的运动随温度上升而变慢，说明在高温下为防止水分子进入疏水胶束壳内，这些栅栏层的质子堆积的更紧密. 同时分子中其他质子的T₂值随温度上升而增长，表现出正常的分子运动的温度效应.     

丙烯腈γ辐射聚合的NMR研究

用¹H NMR、¹³C NMR谱、自旋-晶格弛豫时间（T₁）和自旋-自旋弛豫时间（T₂）研究了丙烯腈在⁶⁰Co γ射线辐射聚合后的大分子结构变化与大分子链的运动. 结果表明随着辐射剂量增大，在单体形成聚合物的过程中，聚合物主链上出现了少量的-OH基团，继续增大辐射剂量， -OH部分被氧化. 对聚合物溶液的变温氢谱的研究表明，溶剂中的残余水与上述-OH形成氢键，且随着温度升高氢键被破坏，同时H₂O与-OH之间还存在着质子交换. 利用¹³C NMR谱对丙烯腈辐射聚合的产物进行了序列结构分析. 对T₁和T₂的研究表明，辐射剂量的增大并未影响到聚丙烯腈的链运动，证明了在丙烯腈的辐射聚合过程交联反应未发生.     

邻苯二甲酸二甲酯系材料中α-弛豫的降温介电谱测量与分析

对邻苯二甲酸二甲酯(dimethyl phthalate)、邻苯二甲酸二乙酯(diethyl phthalate)、邻苯二甲酸二丁酯(dibutyl phthalate)和邻苯二甲酸二异辛酯 (dioctyl phthalate)系列材料中, α-弛豫的降温介电谱进行了测量, 得出了相应材料α-弛豫的平均弛豫时间τ_α^a 随温度T的变化关系. 通过τ_α^a 的实验结果与经验的Vogel-Fulcher-Tammann)定律τ_α^a = τ_α⁰ exp (A/(T-T₀))的拟合, 获得了上述系列材料的τ_α⁰, A和T₀. 分析发现, 随邻苯二甲酸二甲酯系列分子侧链中碳原子数目n的变化, 材料的τ_α⁰, A, T₀ 和T_g 表现出一定的规律性, 具体为随n的增加, 即分子内部自由度的增多, A和T_g 都表现出近乎相同的先减后再增的趋势, 而1/τ_α⁰ 和T₀ 则表现出基本相同的先快速减小, 然后保持基本上不变的趋势. 关键词： 玻璃化转变 介电谱 α-弛豫')" href="#">α-弛豫 邻苯二甲酸二甲酯系列材料     

两个非离子表面活性剂复配体系的NMR研究

通过核磁共振（NMR）技术对NP-10/Tween40和NP-10/C₁₀E₆两个复配体系在不同比例下混合胶束的排列方式、相互作用点及其不同分子间与相同分子间的作用变化进行了研究和比较.二维NOESY实验结果证明了：（1）这两种复配体系的相互作用是随混合比例的不同而变化的;（2）两个复配体系的不同分子间相互作用点有相同之处,但NP-10/Tween40分子间相互作用大于NP-10/C₁₀E₆.横向弛豫时间（T₂）表明,当NP-10/Tween40和NP-10/C₁₀E₆体系的混合比分别为1：2和1：4后,其不同分子间的相互作用开始减小,相同分子间作用开始起主导作用,暗示了复配体系中的理想混合配比和协同效应的变化.横向弛豫时间与纵向弛豫时间之比（T_R=T₂/T₁）反映了与NP-10/C₁₀E₆相比,NP-10/Tween40混合胶束分子链的运动受限更加严重.空间距离计算结果也佐证了NP-10/Tween40和NP-10/C₁₀E₆复配体系的较为理想的配比分别为1：2和1：4;NP-10/Tween40不同分子间距离小于NP-10/C₁₀E₆.     

基于磁共振弛豫时间实现加权像和压脂技术

磁共振成像是根据生物磁性核在磁场中表现的共振特性进行成像的新技术,其中弛豫时间是实现和控制成像的重要物理量.本文使用磁共振成像实验仪,对相关样品的纵向弛豫时间T₁、横向弛豫时间T₂进行测量,并且基于不同弛豫时间采用自旋回波序列实现T₁、T₂加权像,用反转恢复成像序列实现磁共振成像对脂肪的抑制.     

正十二烷基硫酸钠在聚丙烯酰胺溶液中聚集的1H NMR研究

利用核磁共振自旋-晶格弛豫时间（T₁）、自旋-自旋弛豫时间（T₂）、自扩散系数（D）以及二维核Overhause增强谱（2D NOESY）技术研究了表面活性剂正十二烷基硫酸钠（SDS）在聚丙烯酰胺（PAM）浓度固定为10 g/L水溶液中的聚集. 结合与SDS水溶液体系核磁共振实验数据比较,得到了如下信息：（1） 当溶液中有PAM存在时,SDS分子的运动性下降,临界聚集浓度提前;（2） 随着SDS浓度的增加,PAM分子的自扩散性能下降,同时分子链的柔软性也下降了;（3） 2D NOESY谱结果表明,PAM与SDS分子间未发生直接的缔合作用.     

Effect of Ethanol on the Partition Coefficient Of Cyclohexylacetate Between Bulk and Cetyltrjmethylammonium Bromide Micellar Pseudophases

Variation of the partition coefficient of cyclohexylacetate (CA) was studied by a differential absorption spectroscopic method as a function of ethanol and (CTAB) cetyltrimethylammoniumbromide concentrations. Approach used was based upon the pseudo-two phase model, including effect of ethanol concentrations on the critical micelle concentration (CMC) of CTAB. Ethanol enhanced micelle formation of CTAB at concentrations below 1% by volume, had a slight inhibitory effect at higher concentrations and totally inhibited at a concentration above 15% by volume.

Various amounts of ethanol were used with a purpose of changing the solubility of CA in water. The differential absorbance (AA), was almost zero at low concentrations of CTAB, however an increase in AA began at a certain concentration of CTAB which can accordingly be assumed to be consistent with CMC of CTAB in the presence of ethanol. As CTAB concentration increased above CMC, ΔA reached a plateau. In this plateau, ΔA can reasonably be interpreted as the saturation of CA in micellar phase.

Plateau values of ΔA decreased with increasing ethanol concentration. This showed that the fraction of CA in the micellar phase depended on the ethanol concentration in terms of changing the solubility. Partition coefficients, K_c, were obtained from the plots of 1/ΔA against 1/[C_CA] +[C³ _m], which were linear in high CTAB concentrations. It was also seen that as ΔA, K_c decreased when the ethanol percentage were increased. In other words, the lower the solubility of CA in the bulk, the higher the partition coefficient.     

Transverse water relaxation in whole blood and erythrocytes at 3T, 7T, 9.4T, 11.7T and 16.4T; determination of intracellular hemoglobin and extracellular albumin relaxivities

Blood is a physiological substance with multiple water compartments, which contain water-binding proteins such as hemoglobin in erythrocytes and albumin in plasma. Knowing the water transverse (R₂) relaxation rates from these different blood compartments is a prerequisite for quantifying the blood oxygenation level-dependent (BOLD) effect. Here, we report the Carr-Purcell-Meiboom-Gill (CPMG) based transverse (R_2CPMG) relaxation rates of water in bovine blood samples circulated in a perfusion system at physiological temperature in order to mimic blood perfusion in humans. R_2CPMG values of blood plasma, lysed packed erythrocytes, lysed plasma/erythrocyte mixtures, and whole blood at 3 T, 7 T, 9.4 T, 11.7 T and 16.4 T were measured as a function of hematocrit or hemoglobin concentration, oxygenation, and CPMG inter-echo spacing (τ_cp). R_2CPMG in lysed cells showed a small τ_cp dependence, attributed to the water exchange rate between free and hemoglobin-bound water to be much faster than τ_cp. This was contrary to the tangential dependence in whole blood, where a much slower exchange between cells and blood plasma applies. Whole blood data were fitted as a function of τ_cp using a general tangential correlation time model applicable for exchange as well as diffusion contributions to R_2CPMG, and the intercept R_20blood at infinitely short τ_cp was determined. The R_20blood values at different hematocrit and the R_2CPMG values of lysed erythrocyte/plasma mixtures at different hemoglobin concentration were used to determine the relaxivity of hemoglobin inside the erythrocyte (r_2Hb) and albumin (r_2Alb) in plasma. The r_2Hb values obtained from lysed erythrocytes and whole blood were comparable at full oxygenation. However, while r_2Hb determined from lysed cells showed a linear dependence on oxygenation, this dependence became quadratic in whole blood. This possibly suggests an additional relaxation effect inside intact cells, perhaps due to hemoglobin proximity to the erythrocyte membrane. However, we cannot exclude that this is a consequence of the simple tangential model used to remove relaxation contributions from exchange and diffusion. The extensive data set presented should be useful for future theory development for the transverse relaxation of blood.     

Chemical exchange of hydroxyl protons in quercetin measured by pulsed field gradient NMR

The diffusion behavior of hydroxyl protons (OH) in quercetin in 100% DMSO-d₆ (deuterium dimethylsulfoxide) and a 90% DMSO-d₆ solution containing 10% H₂O was investigated with 600 MHz ¹H pulsed field gradient (PFG) nuclear magnetic resonance (NMR). Only resonances of the 5-hydroxyl protons (OH5) were well resolved in NMR spectra of quercetin for all solutions under study. This phenomenon is explained by the intramolecular hydrogen bonding between OH5 protons and the 4-carbonyl oxygen (CO4). During diffusion experiments, the OH5 protons showed a biexponential diffusion decay, indicating an exchange process with water. As water content in the solvents increased, the lifetime (τ _q) of the OH5 protons decreased from 96.7±10.0 ms in 100% DMSO-d₆ to 14.3±1.4 ms in the 90% DMSO-d₆ solution containing 10% H₂O, indicating an increase in the exchange rate (k _q = l/τ _q) of the OH5 protons. This study demonstrates that the diffusion approach with PFG-NMR is much faster and easier for estimating the short lifetime or fast exchange rate of hydroxyl protons in quercetin.     

N.M.R. Spectral Studies of Some Quinolone Derivatives. Part VI.1 N-Methyl-2-Quinolone Derivatives

The chemical shifts of the N-CH₃ protons for a series of 1-methyl-2-quinolone derivatives has been studied. Compounds with an 8-methyl substituent exhibit a slight downfield shift.     

Separation of Anisotropy and Exchange Broadening Using N CSA–N–H Dipole–Dipole Relaxation Cross-Correlation Experiments

Based on the measurement of cross-correlation rates between ¹⁵N CSA and ¹⁵N–¹H dipole–dipole relaxation we propose a procedure for separating exchange contributions to transverse relaxation rates (R₂ = 1/T₂) from effects caused by anisotropic rotational diffusion of the protein molecule. This approach determines the influence of anisotropy and chemical exchange processes independently and therefore circumvents difficulties associated with the currently standard use of T₁/T₂ ratios to determine the rotational diffusion tensor. We find from computer simulations that, in the presence of even small amounts of internal flexibility, fitting T₁/T₂ ratios tends to underestimate the anisotropy of overall tumbling. An additional problem exists when the N–H bond vector directions are not distributed homogeneously over the surface of a unit sphere, such as in helix bundles or β-sheets. Such a case was found in segment 4 of the gelation factor (ABP 120), an F-actin cross-linking protein, in which the diffusion tensor cannot be calculated from T₁/T₂ ratios. The ¹⁵N CSA tensor of the residues for this β-sheet protein was found to vary even within secondary structure elements. The use of a common value for the whole protein molecule therefore might be an oversimplification. Using our approach it is immediately apparent that no exchange broadening exists for segment 4 although strongly reduced T₂ relaxation times for several residues could be mistaken as indications for exchange processes.     

Proton diffusion in the superprotonic phase of [(NH4)1 − xRbx]3H(SO4)2 as studied by 1H spin-lattice relaxation

Proton diffusion in [(NH₄)_1 ? xRb_x]₃H(SO₄)₂ (0 < x < 1) has been studied by means of ¹H spin-lattice relaxation times, T₁. The relaxation times were measured at 200.13 MHz in the range of 296–490 K and at 19.65 MHz in the range of 300–470 K. In the high-temperature phase (phase I), translational diffusion of the acidic protons relaxes both the acidic protons and the ammonium protons. Spin diffusion averages the relaxation rate of the two kinds of protons, whereas proton exchange between them are slow. The spin-lattice relaxation times in phase I were analyzed theoretically, and parameters of proton diffusion were obtained. The mean residence time of the acidic protons increases with increase in x for [(NH₄)_1 ? xRb_x]₃H(SO₄)₂ (0 ≤ x ≤ 0.54). Rb₃H(SO₄)₂ does not obey this trend. The results of NMR well explain the macroscopic proton conductivity.     

Exchange-mediated contrast in CEST and spin-lock imaging

Purpose

Magnetic resonance images of biological media based on chemical exchange saturation transfer (CEST) show contrast that depends on chemical exchange between water and other protons. In addition, spin–lattice relaxation rates in the rotating frame (R_1ρ) are also affected by exchange, especially at high fields, and can be exploited to provide novel, exchange-dependent contrast. Here, we evaluate and compare the factors that modulate the exchange contrast for these methods using simulations and experiments on simple, biologically relevant samples.

Methods

Simulations and experimental measurements at 9.4 T of rotating frame relaxation rate dispersion and CEST contrast were performed on solutions of macromolecules containing amide and hydroxyl exchanging protons.

Results

The simulations and experimental measurements confirm that both CEST and R_1ρ measurements depend on similar exchange parameters, but they manifest themselves differently in their effects on contrast. CEST contrast may be larger in the slow and intermediate exchange regimes for protons with large resonant frequency offsets (e.g. > 2 ppm). Spin-locking techniques can produce larger contrast enhancement when resonant frequency offsets are small (< 2 ppm) and exchange is in the intermediate-to-fast regime. The image contrasts scale differently with field strength, exchange rate and concentration.

Conclusion

CEST and R_1ρ measurements provide different and somewhat complementary information about exchange in tissues. Whereas CEST can depict exchange of protons with specific chemical shifts, appropriate R_1ρ-dependent acquisitions can be employed to selectively portray protons of specific exchange rates.     

Efficient spin diffusion of transverse13C magnetization

Relatively efficient spin diffusion among unprotonated carbons with large chemical-shift anisotropies can be achieved by a¹³C nuclear magnetic resonance multiple-pulse sequence with a lowduty cycle of ～5% on the¹³C channel, which minimizes sample heating and reduces cumulative effects of pulse imperfections. The spin diffusion occurs among transverse-magnetization isochromats, while the total transverse magnetization is a conserved quantity under the average Hamiltonian. The “flip-flop” term of the dipolar-coupling average Hamiltonian is the same as in the full dipolar coupling, i.e., its scaling factor is unity. For a sample of 40%¹³COO-labeled poly(vinyl acetate), with¹³C in ester groups accounting for 7% of all heavy atoms, magnetization equilibrates within 20 ms over a volume of (0.9 nm)³, corresponding to a molecular mass of 500 Da, while the T₂ relaxation time of the total transverse magnetization is ～40 ms. The spin diffusion coefficient is estimated asD = 3 ± 1.5 nm²/s.     

Proton diffusion in the room-temperature phase of [(NH4)1−xRbx]3H(SO4)2 as studied by 1H spin-lattice relaxation in the rotating frame

Proton diffusion in the room-temperature phase (phase II) of [(NH₄)_1?xRb_x]₃H(SO₄)₂ (0≤x≤1) has been studied by means of ¹H spin-lattice relaxation times in the rotating frame, T_1ρ. The ¹H T_1ρ values were measured at 200.13 MHz in the range of 380–490 K. The ammonium protons and the acidic protons have independent T_1ρ values in the higher temperature range of phase II, suggesting that the spin diffusion between the two species is ineffective. The translational diffusion of the acidic protons is the most dominant mechanism to relax both the ammonium protons and the acidic protons in phase II. The ¹H T_1ρ values in phase II are analyzed theoretically and the motional parameters are obtained. The results of NMR well explain the macroscopic proton conductivity.