​To determine the pharmacological profiles of the peptides studied in the laboratory and in particular those that are highly reticulated, we have optimized their solid-phase peptide synthesis (SPPS) and refolding processes. SPPS allows us to make engineering of the desired molecules, including specific fluorescent or radioactive labeling, sequence modifications (variants for structure-activity relationships, deimmunization attempt or pharmacodynamic optimization), or multiple functionalization. Introduction of non-natural amino acids (biotinylation, azido moiety able to react with an alkyne for peptidomimetic compounds…), post-translational modifications (C-terminal amidation, hydroxy-proline, tyrosine sulfate…), endosomal escape domains insertion (to make a peptide able to cross the membrane barrier) are the main modifications we introduce in our molecules. These changes influence the stability or functional properties of the toxins studied and reinforce their exploitation as imaging or therapeutic agents (Salinas et al., 2021) (Droctove et al., 2020) (Mourier et al., 2016) (Fruchart-Gaillard et al., 2012).

​