Peptidomimetics - An infinite reservoir of metal binding motifs in metabolically stable and biologically active molecules

The involvement of metal ions in interactions with therapeutic peptides is inevitable. They are one of the factors able to fine-tune the biological properties of antimicrobial peptides, a promising group of drugs with one large drawback - a problematic metabolic stability. Appropriately chosen, proteolytically stable peptidomimetics seem to be a reasonable solution of the problem, and the use of D-, beta-, gamma-amino acids, unnatural amino acids, azapeptides, peptoids, cyclopeptides and dehydropeptides is an infinite reservoir of metal binding motifs in metabolically stable, well-designed, biologically active molecules. Below, their specific structural features, metal-chelating abilities and antimicrobial potential are discussed.

Automated summary

The involvement of metal ions in interacting with therapeutic peptides can fine-tune the biological properties of antimicrobial peptides. The use of proteolytically stable peptidomimetics, such as D-, beta-, gamma-amino acids, unnatural amino acids, azapeptides, peptoids, cyclopeptides, and dehydropeptides, provides an infinite reservoir of metal binding motifs for metabolically stable, well-designed, biologically active molecules. This approach offers potential solutions to the problematic metabolic stability of therapeutic peptides.