Myoglobin embedded in saccharide amorphous matrices: water-dependent domains evidenced by small angle X-ray scattering

Abstract

We report Small Angle X-ray Scattering (SAXS) measurements performed on samples of carboxy-myoglobin (MbCO) embedded in low-water trehalose glasses. Results showed that, in such samples, "low-protein" trehalose-water domains are present, surrounded by a protein-trehalose-water background; such finding is supported by Infrared Spectroscopy (FTIR) measurements. These domains, which do not appear in the absence of the protein and in analogous sucrose systems, preferentially incorporate the incoming water at the onset of rehydration, and disappear following large hydration. This observation suggests that, in organisms under anhydrobiosis, analogous domains could play a buffering role against the daily variations of the atmospheric moisture. The reported results are rationalized by assuming sizably different protein-matrix coupling in trehalose with respect to sucrose, analogous to the one suggested for the photosynthetic reaction centre from Rhodobacter sphaeroides (F. Francia et al., J. Am. Chem. Soc., 2008, 130, 10240-10246).