| The development of a catalyst that enantioselectively attacks peptides derived from D-amino acids at a faster rate than those derived from L-amino acids is unknown. As previously mentioned, D-amino acids are the key components of the bacterial cell wall. Due to the fact that bacteria use D-amino acids in peptides, specifically in the peptidoglycan of their cell walls, and mammals do not, this methodology represents a potentially novel mode of action for antibiotics.;R-CDPy3 complex was synthesized in order to mimic the activity of N4Py and especially Bn-TPEN (due to its structural similarity) in the cleavage of peptides. Two derivatives of the R-CDPy3 (R = Me, Et) ligand were prepared by inserting the methyl and ethyl groups instead of the benzyl which generate a less sterically hindered ligand. These two new ligands were successful in generating the FeII and the FeIVO complexes. These iron-based catalysts will be tested toward the oxidative cleavage of the backbone of amino acids and peptides.;On the other hand, we have generated a new CoIII complex derived from Bn-CDPy3. Interestingly, only one coordination geometry out of five possible modes of coordination was favored. |
