Concentration Dependence of Elastic and Viscoelastic Properties of Aqueous Solutions of Ficoll and Bovine Serum Albumin by Brillouin Light Scattering Spectroscopy.

The cellular environment is crowded with macromolecules of different shapes and sizes. The effect of this macromolecular crowding has been studied in a variety of synthetic crowding environments: two popular examples are the compact colloid-like Ficoll macromolecule and the globular protein bovine serum albumin (BSA). Recent studies have indicated that a significant component of bound or surface-associated water in these crowders reduces the available free volume. In this work, Brillouin light scattering experiments were performed on aqueous solutions of Ficoll 70 and Ficoll 400 with concentrations ranging from 1 to 35 wt % and BSA with concentrations of 1 to 27 wt %. From the dependence of spectral peak parameters on polymer concentration, we determined fundamental solution properties: hypersound velocity, adiabatic bulk modulus and compressibility, apparent viscosity, and hypersound attenuation. The existing theory that ignores intermolecular interactions can capture only the observed linear trends in the frequency shift up to a threshold concentration, beyond which a quadratic term accounting for intermolecular interactions is necessary. This likely indicates a transition from the dilute to semidilute regime. In the Ficoll solutions (but not BSA), we see evidence for a central mode, which is indicative of relaxation in the hydration shell of Ficoll.

Temperature dependence of the viscoelastic properties of a natural gastropod mucus by Brillouin light scattering spectroscopy.

Brillouin spectroscopy was used to probe the viscoelastic properties of a natural gastropod mucus at GHz frequencies over the range -11 °C ≤ T ≤ 52 °C. Anomalies in the temperature dependence of mucus longitudinal acoustic mode peak parameters and associated viscoelastic properties at T = -2.5 °C, together with the appearance of a peak due to ice at this temperature, suggest that the mucus undergoes a phase transition from a viscous liquid state to one in which liquid mucus and solid ice phases coexist. Failure of this transition to proceed to completion even at -11 °C is attributed to glycoprotein-water interaction. The temperature dependence of the viscoelastic properties and the phase behaviour suggest that water molecules bind to glycoprotein at a temperature above the onset of freezing and that the reduced ability of this bound water to take on a configuration that facilitates freezing is responsible for the observed freezing point depression and gradual nature of the liquid-solid transition.