Search

Highly complex, multicomponent gels and water-containing soft materials have varied applications in biomedical, pharmaceutical, and food sciences, but the characterization of these nanostructured materials is extremely challenging. The aim of this study was to use stearoyl macrogol-32 glycerides (Gelucire 50/13) gels containing seven different species of glycerides, PEG, and PEG-esters, as model, complex, multicomponent gels, to investigate the effect of water content on the micro- and nanoarchitecture of the gel interior. Thermal analysis and NMR relaxometry were used to probe the thermal and diffusional behavior of water molecules within the gel network. For the highly concentrated gels (low water content), the water activity was significantly lowered due to entrapment in the dense gel network. For the gels with intermediate water content, multiple populations of water molecules with different thermal responses and diffusion behavior were detected, indicating the presence of water in different microenvironments. This correlated with the network architecture of the freeze-dried gels observed using SEM. For the gels with high water content, increased quantities of water with similar diffusion characteristics as free water could be detected, indicating the presence of large water pockets in these gels. The results of this study provide new insights into structure of Gelucire gels, which have not been reported before because of the complexity of the material. They also demonstrate that the combination of thermal analysis and NMR relaxometry offers insights into the structure of soft materials not available by the use of each technique alone. However, we also note that in some instances the results of these measurements are overinterpreted and we suggest limitations of the methods that must be considered when using them.

We present a minor but essential modification to the CODEX 1D-MAS exchange experiment. The new CONTRA method, which requires minor changes of the original sequence only, has advantages over the previously introduced S-CODEX, since it is less sensitive to artefacts caused by finite pulse lengths. The performance of this variant, including the finite pulse effect, was confirmed by SIMPSON calculations and demonstrated on a number of dynamic systems.

The behaviour of water in the presence of proteins and DNA as elucidated by nuclear magnetic resonance is reviewed. The picture that emerges is that in dilute solution only those water molecules in the interior of the biopolymers or in clefts have their motions substantially affected. In concentrated systems the situation is more complicated because many more motions have to be considered, but there is no evidence of special effects due to the biopolymers being present. The case of nonfreezing water in protein solutions is considered, and it is suggested that this is not evidence for 'bound' water but simply due to the effects of the inhibition of protein precipitation.

The solid state 13C CPMAS NMR spectra of plant cell walls are often complex owing to superposition of resonances from different polysaccharides and the heterogeneity of the cell wall assembly. In this paper, we describe the application of a set of proton relaxation-induced spectral editing (PRISE) experiments which combine 1H relaxation properties (T1, T1rho, T2) with 13C high resolution spectroscopy (CPMAS) to relate the dynamics of the plant cell walls and model systems to their domain structural details. With PRISE it has been found that in plant cell wall materials, cellulose is always associated with the long components of spin-lattice relaxation in both the laboratory and rotating frames whereas non-cellulose polysaccharides (pectin and hemicellulose) are associated with the short ones. For the proton T2 relaxation, cellulose is only associated with the short component (below 20 micros), pectin contributes to both the short component and the long one.

The molecular motions of D-alpha-galacturonic acid monohydrate (GA) and its derivative methyl-alpha-D-galacturonic acid methyl ester monohydrate (MGAM) in the solid state have been studied using 1H NMR. Both protonated and deuterium exchanged samples have been used. Spin-lattice relaxation times in the laboratory and rotating frames as well as second moments have been measured over the temperature range 90-370 K. Analysis of results has shown that in GA spin-lattice relaxation is chiefly by hydroxyl groups and water of crystallization. In MGAM, methyl groups dominate spin-lattice relaxation in the laboratory frame at the low temperature. Hydroxyl groups and water of crystallization contribute to the spin-lattice relaxation in the laboratory frame in the high temperature region. In the rotating frame motion of hydroxyl groups and water of crystallization provide the main relaxation pathway. Changes in the static second moment with temperature can be reasonably well predicted using values of correlation time and motionally averaged second moments obtained by fitting the spin-lattice relaxation data. 13C CPMAS spectra for GA and MGAM are also described.

An analysis of the possible modes of motion of water molecules in polysaccharide gels indicates that the interpretation of NMR results does not require the supposition of a class of 'bound water' with highly perturbed motional states. There may, however, be water molecules associated with junction zones in the gels whose motions are restricted either by incorporation into the molecular secondary structure or as interstitial water in crystallites. Hydration and dehydration effects as well as the phenomenon of non-freezing water may all be explained within a framework of well understood processes. It is concluded that there is no requirement to appeal to 'bound water' to explain any of the properties of water in polysaccharide gels.

The hydration behaviour of a purified high-M(r) subunit of glutenin has been studied using Fourier transform infra-red (FTIR) and nuclear magnetic resonance (NMR) spectroscopy. The water-insoluble protein was examined in an unalkylated form with intermolecular disulfide bonds, and in a reduced and alkylated (unpolymerized) form. Hydration produced a marked increase in chain mobility, especially above a threshold water content of about 37% w/w. NMR experiments also showed that some parts of the chain were held in a much less mobile state, even at higher water contents. Little difference could be seen between alkylated and unalkylated subunits, implying that NMR is sensitive to localized motions, but not to any restrictions imposed by disulfide bridges close to the chain ends. FTIR spectra of the protein films have shown that increasing hydration enables changes to occur in favour of a more extended and beta-sheet-type structure. The changes in secondary structure are very noticeable at water contents corresponding to the NMR mobility threshold. The behaviour is influenced by intermolecular interactions. beta-sheet formation is enhanced by the presence of disulfide bonds in the unalkylated samples. There is little evidence of beta-structure (sheet or extended chain) either in the dry state, where protein-protein interactions are strongest, or in dilute acetic acid solution, where the interactions are weakest. The balance between protein-protein and protein-water hydrogen-bonding interactions therefore appears to influence the formation of beta-sheet and extended chain structures, and these may in turn affect the elasticity of high M(r) subunits.

The CP/MAS 13C NMR spectra of crystalline L-leucine and DL-leucine at 7 T are compared with previously reported spectra at lower field strengths. An increasing dominance of chemical shift effects over residual 14N-13C dipolar interactions is observed on the C alpha and C beta splittings with increasing field strength. A new structure is observed in the 25 ppm region of both samples. The spectra in this region were assigned by application of the depolarisation-repolarisation method. The assignment showed differences in the ordering of peaks between solid state and liquid state chemical shifts.

A stochastic computer simulation is used to investigate the effects of restricted diffusion in NMR microscopy. It is shown that diffusion contributes to a loss of interfacial resolution through two main mechanisms. The first applies to spatial regions bound by impermeable interfaces and involves diffusive averaging of the frequency differences set up by the applied field gradients. This effect can be made arbitrarily small by increasing the magnitude of the field gradient. The second mechanism involves diffusion through permeable membranes or interfaces defining the sample morphology. This effect can, in principle, be reduced by multiple echo imaging with short pulse spacings. The possibility of imaging diffusive flow through a permeable interface is discussed.

A 31P topical magnetic resonance study of whole chicken's eggs in vivo is described. Resonances from adenosine triphosphate, phosphocreatine, inorganic phosphate and phosphorous storage protein were observed. These changed in relative intensity as the embryo developed. No ill effects due to exposure to radiofrequency radiation or magnetic fields were observed. It is concluded that topical magnetic resonance can make a useful contribution to the study of embryonic development in avian eggs.