Agarose samples of low (Ag1) and high (Ag2) O -methyl content on position 6 of the galactose residue were studied in H2O and D2O. Differential scanning calorimetry, turbidity and rheological measurements showed a [Formula: see text] 2 ° C shift in the coil-to-helix transition temperature, indicating higher helix stability in D2O. The differential scanning calorimetry data could be superimposed using a temperature shift factor, suggesting similar extents of helix aggregation in both solvents. Small angle X-ray scattering of H2O and D2O gels were essentially identical, indicating no change in the small scale ( [Formula: see text] 0.05-20 nm) network structure on isotopic exchange. Larger ([Formula: see text] 1 μm) scale heterogeneities were more pronounced in deuterium gels. The 1HT2 relaxation times were measured at different H/D ratios. These relaxation times were analyzed using a model assuming regular solution mixing of H2O, HDO and D2O between the solvent and gel phases. The fit results suggested that H2O has higher affinity for the agarose network than HDO and D2O. The difference, however, was much larger for the Ag2 sample. This finding implies that the higher hydrophobic effect observed in D2O affects the hydration state much more strongly for the more hydrophobic (and more polarizable) agarose sample Ag2. As a consequence, Ag2 (but not Ag1) gels retained more H2O than D2O. In contrast, the bulk rheology of either hydrogel was not affected by the isotopic exchange.
Keywords: Soft Matter: Polymers and Polyelectrolytes.