The intra and intermolecular interactions maintaining these macromolecular or supramolecular structures are all non-covalent interactions (electrostatic interactions, H bonds, van der Waals forces, hydrophobic effect). It is the summation of these multiple low energy interactions that gives stability to these buildings, but also their flexibility and dynamics since these interactions can fluctuate rapidly under the effect of temperature, pH, ionic strength, etc. ... The formation of these buildings is generally cooperative, which makes it difficult to quantify the different types of interaction individually since they are set up simultaneously.
Particularly fascinating examples are provided by the viruses: in the cells that they infect, they are able to set up or manipulate complex supramolecular buildings with a remarkable economy of means (sometimes by the expression of a single protein ). In addition to their medical or veterinary importance, viruses provide very fertile study systems. The other major line of research of the team is the spontaneous self-assembly of therapeutic peptides, again with the double interest of discovering new formulations and understanding the underlying molecular mechanisms at the most fundamental level. In these two areas of research, a major component is the interactions between proteins and membranes (how viruses manipulate cell membranes, how therapeutic peptides can cross them).
The team's activity focuses on the identification and characterization of non-covalent molecular interactions guiding peptide and protein assemblies, the quantification of interaction energies and the understanding of the intermediate stages of implementation of the final architectures ( characterization, kinetics of formation and stability of intermediate buildings).