A strategy combining combinatorial chemistry and an activity-based screening leads to the development of a peptidyl catalytic drug that reduces the oxidative stress in cellular models.

Histidine-rich tripodal peptides form unique oligonuclear complexes with copper(ii), which exhibit efficient catecholase-like activity.

In order to develop a minimalist chemical model of matrix metalloproteinases (MMPs), we Around pH 6-7 the peptide, similarly to MMPs, offers {3N im } coordinated binding site for both zinc(II) and copper(II). In the case of copper(II), the formation of amide coordinated species at higher pH ceased the analogy with the copper(II) containing MMP variant. On the other hand, the zinc(II)-peptide system mimics some basic features of the MMP active sites: the main species around pH 7 (ZnH 2 L) possesses {3N im ,H 2 O} coordination environment, the deprotonation of the zinc-bound water takes place near to the physiological pH, it forms relatively stable ternary complexes with hydroxamic acids, and the species ZnH 2 L(OH) and ZnH 2 L(OH) 2 have notable hydrolytic activity between pH 7-9.