Protein Hydration in a Bioprotecting Mixture

We combined broad-band depolarized light scattering and infrared spectroscopies to study the properties of hydration water in a lysozyme-trehalose aqueous solution, where trehalose is present above the concentration threshold (30% in weight) relevant for biopreservation. The joint use of the two different techniques, which were sensitive to inter-and intra-molecular degrees of freedom, shed new light on the molecular mechanism underlying the interaction between the three species in the mixture. Thanks to the comparison with the binary solution cases, we were able to show that, under the investigated conditions, the protein, through preferential hydration, remains strongly hydrated even in the ternary mixture. This supported the water entrapment scenario, for which a certain amount of water between protein and sugar protects the biomolecule from damage caused by external agents.

Thermodynamics of Concanavalin A Self-Association in the Presence of Osmolytes

Protein-protein interactions are critical for biological function and depend significantly on environmental factors. A wide variety of small organic molecules that comprise the cellular environment are capable of interacting with proteins to affect folding, binding, and association. The plant lectin concanavalin A (ConA) undergoes a reversible, pH dependent dimer-to-tetramer equilibrium and has been used in our laboratory as a model system to study the effect of osmolytes on protein self-association. Previous research determined that trimethylamine N-oxide (TMAO) stabilizes the tetrameric conformation, while urea favors the dimer. Studying the equilibrium over a range of temperatures allowed quantification of the enthalpy change (∆H) and entropy change (∆S) of tetramer formation. Urea increased both the ∆H and ∆S of tetramer formation, while TMAO decreased both. These effects are consistent with preferential hydration of the dimer-dimer interface in TMAO solution and preferential binding of urea to the interface. KEYWORDS: Concanavalin A; Osmolytes; Trimethylamine N-oxide; Urea; Protein-Protein Interaction; Equilibrium; Enthalpy; Preferential Hydration

Stabilizing effect of TMAO on globular PNIPAM states: preferential attraction induces preferential hydration

We study the effect of the organic co-solute trimethylamine N-oxide (TMAO) on the volume phase transition of microgel particles made from poly(N-isopropylacrylamide) (PNIPAM) using dynamic light scattering (DLS) and all-atom molecular dynamics (MD) simulations.

Folding propensity of intrinsically disordered proteins by osmotic stress

Preferential hydration changes accompanying the osmotic folding of two intrinsically disordered proteins (IDPs) were determined.