Abstract: Immobilization of proteins and other biomolecules in saccharide matrices leads to a series of peculiar properties that are relevant from the point of view of both biochemistry and biophysics, and have important impli-cations on related fields such as food industry, pharmaceutics, and medicine. In the last years, the properties of biomolecules embedded into glassy matrices and/or highly concentrated solutions of saccharides have been thor-oughly investigated, at the molecular level, through in vivo, in vitro, and in silico studies. These systems show an outstanding ability to protect biostructures against stress conditions; various mechanisms appear to be at the basis of such bioprotection, that in the case of some sugars (in particular trehalose) is peculiarly effective. Here we review recent results obtained in our and other laboratories on ternary protein- sugar-water systems that have been typically studied in wide ranges of water content and temperature. Data from a large set of complementary experimental techniques provide a con-sistent description of structural, dynamical and functional properties of these systems, from atomistic to thermodynamic level. In the emerging picture, the stabilizing effect induced on the encapsulated systems might be attributed to a strong biomolecule-matrix coupling, mediated by extended hydrogen-bond networks, whose specific properties are determined by the saccharide composition and structure, and depend on water content.

eric) a and eatu s aim Na eties in the polymeric structure is proposed to be directly involved in the protein inactivation rtificia ng from transf t num bility a cial oxygen carriers that could solve the above mentioned donor transfusion associated drawbacks. Among Hb based cellular systems, the use of polymeric nano-particles as artificial oxygen carriers presents many advantages mainly related to the feasibility of co-encapsulating reducing agents that can avoid Hb oxidation during the formulation process, hydrophilic ionizable acid group, a hydrophobic but potentially degradable ester residue, and an alkyl ether moiety. The polymer water solubility gradually increases under physiological conditions, thanks to the progressive carboxyl ionization and to an autocata-lytic or enzyme mediated ester hydrolysis (Woodruff et al., 1972; Vert et al., 1992). Furthermore, the presence of PEG moieties even-tually grafted onto the polymermatrix confers to the functionalised system stealth properties. The present study is aimed at investigating the maintenance of Hb structural and functional features after its loading into

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form 4 of protein structure (i.e., tertiary vs. quaternary) and from its ligation state. Decoupling the protein quaternary used to find quaternary structure sensitive spectroscopic markers. Iron–cobalt hybrid hemoglobins have also been investigated to study the effects of quaternary structure on Quaternary conformational changes are of utmost importance to protein function. The best known example is probably the TXR transition of hemoglobin, which is responsible for the cooperative ligand binding of this

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