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Aqueous solutions of poly(N-isopropylacrylamide), P-NIPAAm, exhibit a noticeable temperature responsive change in molecular conformation at a cloud point temperature (Tcp). As the temperature rises above Tcp, the extended coil-like P-NIPAAm structure changes into a swollen globule-like conformation as hydration levels decrease and hydrophobic interactions increase. Though water plays an important role in this coil-to-globule transition of P-NIPAAm, the behavior of water molecules and the associated hydrogen-bond (HB) network of the surrounding bulk water are still veiled in uncertainty. In this study, we elucidate changes in the hydration state and the dynamical structure of the water HB network of P-NIPAAm aqueous solutions during the coil-to-globule transition by analyzing the complex dielectric constant in the terahertz region (0.25-12 THz), where bulk water reorientations and intermolecular vibrations of water can be selectively probed. The structural properties of the water HB network were examined in terms of the population of the non-HB water molecules (not directly engaged in the HB network or hydrated to P-NIPAAm) and the tetrahedral coordination of the water molecules engaged in the HB network. We found the hydration number below Tcp (≈10) was decreased to approximately 6.5 as temperature increased, in line with previous studies. The HB network of bulk water becomes more structured as the coil-to-globule phase transition takes place, via decreases in non-HB water and reduction in the orderliness of the tetrahedral HB architecture. Together these results indicate that the coil-to-globule transition is associated with a shift to hydrophobic-dominated interactions that drive thermoresponsive structural changes in the surrounding water molecules.

Terahertz time-domain attenuated total reflection measurements of monosaccharide (glucose and fructose) and disaccharide (sucrose and trehalose) solutions from 0.146 M to 1.462 M were performed to evaluate (1) the hydration state and (2) the destructuring effect of saccharide solutes on the hydrogen bond (HB) network. Firstly, the extent of hydration water was determined by the decreased amount of bulk water with picosecond relaxation time that was replaced by that with much longer orientational relaxation time. As a result, we found glucose and trehalose exhibits stronger hydration capacity than fructose and sucrose, respectively, despite of the same number of the hydroxyl groups. For each saccharide, the hydration number tended to decrease with solute concentration. Secondly, the destructuring effect of these saccharide solutes on the HB network of the surrounding bulk water was discussed from the perspective of the fraction of non-hydrogen-bonded (NHB) water isolated from the HB network. We found the fraction of NHB water molecules that are not engaged in the HB network monotonously increased with saccharide concentration, indicating saccharide solutes promote the disruption of the water HB network. However, no noticeable differences were confirmed in the fraction of NHB water between glucose and fructose or between sucrose and trehalose. In contrast to hydration number, the number of NHB water produced by a single saccharide solute was less dependent on solute concentration, and three monosaccharide/disaccharide solutes were found to produce one/two NHB water molecules.

Recent studies of saccharides' peculiar anti-freezing and anti-dehydration properties point to a close association with their strong hydration capability and destructuring effect on the hydrogen bond (HB) network of bulk water. The underlying mechanisms are, however, not well understood. In this respect, examination of the complex dielectric constants of saccharide aqueous solutions, especially over a broadband frequency region, should provide interesting insights into these properties, since the dielectric responses reflect corresponding dynamics over the time scales measured. In order to do this, the complex dielectric constants of glucose solutions between 0.5 GHz and 12 THz (from the microwave to the far-infrared region) were measured. We then performed analysis procedures on this broadband spectrum by decomposing it into four Debye and two Lorentz functions, with particular attention being paid to the β relaxation (glucose tumbling), δ relaxation (rotational polarization of the hydrated water), slow relaxation (reorientation of the HB network water), fast relaxation (rotation of the non-HB water), and intermolecular stretching vibration (hindered translation of water). On the basis of this analysis, we revealed that the hydrated water surrounding the glucose molecules exhibits a mono-modal relaxational dispersion with 2-3 times slower relaxation times than unperturbed bulk water and with a hydration number of around 20. Furthermore, other species of water with distorted tetrahedral HB water structures, as well as increases in the relative proportion of non-HB water molecules which have a faster relaxation time and are not a part of the surrounding bulk water HB network, was found in the vicinity of the glucose molecules. These clearly point to the HB destructuring effect of saccharide solutes in aqueous solution. The results, as a whole, provide a detailed picture of glucose-water and water-water interactions in the vicinity of the glucose molecules at various time scales from sub-picosecond to hundreds of picoseconds.

Terahertz time-domain attenuated total reflection spectroscopy, in combination with a two-interface model, is used to determine the complex dielectric constants of cultured human cancer cells (DLD-1, HEK293 and HeLa). Picosecond and sub-picosecond water dynamics are dominant in the measured complex dielectric constants of these cells. We demonstrate that dielectric responses below 1.0 THz best characterize the particular water dynamics of cancer cells when compared with extracellular water. Debye-Lorentz fitting revealed that this is due to a significantly attenuated slow relaxation mode and enhanced fast relaxation mode of the water in these cancer cells. These findings could lead to a new procedure to digitally evaluate cellular activities or functions, in terms of intracellular water dynamics, and remove the veil from the mysterious intracellular milieu.

Water conformation around hydrophobic side chains of four amino acids (glycine, L-alanine, L-aminobutyric acid, and L-norvaline) was investigated via changes in complex dielectric constant in the terahertz (THz) region. Each of these amino acids has the same hydrophilic backbone, with successive additions of hydrophobic straight methylene groups (-CH2-) to the side chain. Changes in the degree of hydration (number of dynamically retarded water molecules relative to bulk water) and the structural conformation of the water hydrogen bond (HB) network related to the number of methylene groups were quantitatively measured. Since dielectric responses in the THz region represent water relaxations and water HB vibrations at a sub-picosecond and picosecond timescale, these measurements characterized the water relaxations and HB vibrations perturbed by the methylene apolar groups. We found each successive straight -CH2- group on the side chain restrained approximately two hydrophobic hydration water molecules. Additionally, the number of non-hydrogen-bonded (NHB) water molecules increased slightly around these hydrophobic side chains. The latter result seems to contradict the iceberg model proposed by Frank and Evans, where water molecules are said to be more ordered around apolar surfaces. Furthermore, we compared the water-hydrophilic interactions of the hydrophilic amino acid backbone with those with the water-hydrophobic interactions around the side chains. As the hydrophobicity of the side chain increased, the ordering of the surrounding water HB network was altered from that surrounding the hydrophilic amino acid backbone, thereby diminishing the fraction of NHB water and ordering the surrounding tetrahedral water HB network.

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