Wpływ różnych reszt β-aminokwasowych na zdolności koordynacyjne peptydów wobec jonów metali przejściowych

Peptidomimetics are different groups of compounds which are the modifications of natural occurring peptides - mostly in the sense of the structure. Due to these kind of changes, the new, modified systems are more stable and could act as a tool dedicated in specific biological activity. One of the most important and developed group of peptidomimetics are β-peptides. This review discusses the coordination ability of peptides containing β-amino acid residues incorporated into their sequence. Special attention is given to the importance of βAla residue and metal binding affinity of transition metal ions, especially Cu²⁺ ion. The coordination process occurs analogously to peptides composed of a-amino acids. The complexes are usually formed initially by coordination of N-terminal amine group and subsequently, with increasing pH value, by deprotonation of amide bonds. The main difference can be observed in the stability and geometry of complexes. Namely, the stability constants of β-peptides are usually slightly lower than in the case of natural analogues. Furthermore, the review presents data according to coordination ability of peptides containing β-amino acids, such as: βAsp, βHis, βCys and βLys. In spite of differences between standard peptides and their analogues, containing β-amino acid residues, there are no very important differences in the model of their coordination with the transition metal ions. However, the comparison of β-peptides and their natural counterparts reveals interesting features, which can be useful for more effective designing of new compounds possessing expected properties.