XI Reunião Regional Nordeste da SBBq | 4th International Symposium in Biochemistry of Macromolecules and BiotechnologyStabilization of protein and protein-like molecules translates into preservation of both
structure and functionality during storage and/or targeting, and such stabilization is
mostly attained through establishment of a thermodynamic equilibrium with the
(micro)environment. The basic thermodynamic principles that govern protein structural
transitions and the interactions of the protein and/or peptide molecule with its
(micro)environment will, therefore, be tackled. Protein stabilization is based upon
dampening the molecular motions and, therefore, eliminating conformational transitions
while the molecule is still in the native 3D (folded) state. The 3D structure of a protein
molecule depends mostly on two types of interactions: intramolecular interactions
between aminoacid moieties and intermolecular interactions with solute and/or solvent
molecules present in its microenvironment. Stabilizing a biomolecule (aiming at
preserving its function) involves dampening its molecular motions, and this can be
achieved by reducing the chemical activity of the water present in its microenvironment,
thus stabilizing both its structure and functionality. Recently, the simultaneous
entrapment-stabilization of proteins and enzymes based on nanoencapsulation in a
nanoemulsion (W/O/W) matrix with an hydrophilic core has started to gain momentum.
Similarly to the stabilization mechanism of osmolytes, in nanoencapsulation the water
activity is altered thus affecting the molecular motions of the proteins. Highlights will also
be given to structural and functional stabilization of protein entities (viz. enzymes,
(macro)peptides, (recombinant) proteins, and bacteriophages) by chemical
methodologies. Modification of the biomolecules microenvironment via multipoint
covalent attachment onto a solid surface followed by hydrophylic polymer coimmobilization,
are some of the (latest) strategies that will be discussed.info:eu-repo/semantics/publishedVersio
