Abstract
From biocatalysts such as enzymes, to therapeutic targets and drugs such as membrane proteins and antibodies, various classes of proteins are manipulated outside their natural context. Stabilizing them is often a challenge. We will illustrate how association with synthetic macromolecules can recover, or retain, solubility and activity. The terms "armored" protein or "artificial chaperone" often refer to these protection and renaturation objectives. Complex coulombic and/or amphiphilic assemblies and stimulus-modulated phase transitions form the physico-chemical basis of these approaches, some of whose most recent achievements will be described.
Christophe Tribet
A chemist trained in the physical chemistry of surfactants, polymers and soft matter, C. Tribet's experimental research focuses on the study and control of complexes between artificial macromolecules and proteins. These macromolecular "tools" have applications in pharmaceuticals and biology, notably for the stabilization of therapeutic antibodies, the study of integral membrane proteins, or as substrate coatings for the culture of living cells. Doctor of Sorbonne University (Paris VI University in 1993), then CNRS research fellow at ESPCI (Science et Ingénierie de la matière Molle laboratory), C. Tribet is currently CNRS research director at the École normale supérieure, in the chemistry department.
