This topic focuses on the design, modulation of physicochemical and biological properties and the study of membranotropic peptides or proteins. Cell Penetrating Peptides (CPPs), Antimicrobial Peptides (AMPs) and Antiviral Peptides (AVPs) are our main objects of study. We modify their sequences to identify, at the molecular level, the structural motifs responsible for the different membranotropic activities of these peptides. Our skills in microbiology and cell culture allow us to study and quantify the effect of chemical modifications of AMPs or AVPs on their biological activity. Analytical developments based on mass spectrometry or fluorometry make it possible to quantify the internalization of CPPs in cells.

Calorimetry is used to evaluate the type of interaction of peptides with membrane models and we develop photolabeling approaches coupled with mass spectrometry analysis (PAL-MS) to identify the interaction partners of CPP and AMP in membrane models using photoactivatable CPP, AMP or lipids. Photoactivatable and fluorogenic probes are designed and synthesized to allow the transposition of PAL-MS on cells.

Associated methodologies:

• Affinity photolabeling (fluorogenic or not) coupled with mass spectrometry (PAL-MS) (C. Chieffo, E. Sachon, S. Sagan, A. Walrant)
• Quantifications based on mass spectrometry or fluorometry (F. Burlina, F. Illien, E. Sachon, S. Sagan, A. Walrant)
• Formulation of artificial membranes and cell membranes mimics (C. Chieffo, F. Illien, A. Walrant)
• Bacterial and eucaryotic cell culture (T. Drujon, F. Illien)