Résumé
We obtained the binding free energy of the complex [Co(C
2O
4)
3]
3− to the peptide H–Lys–Gly–(Lys–Gly)
9–Lys–NH
2, and to the monomers (aminoacids) forming the peptide, using the electron transfer reaction between [Ru(NH
3)
5pz]
2+ and [Co(C
2O
4)
3]
3− as the probe. The polymerization of the monomers increases the negative free energy of binding and changes its character, non-cooperative for the monomers and anti-cooperative for the peptide. This increase in the negative free energy represents a driving force for the polymerization process that produces the peptide from the aminoacids (monomers) in such a way that the polymerization in the presence of the cobalt complex is more favourable, from a thermodynamic point of view, in 16.5 kJ/mol.