AI Article Synopsis

  • Metal ions play a crucial role in enhancing the biological properties of antimicrobial peptides, which are promising but often struggle with metabolic stability.
  • To address this stability issue, researchers are exploring peptidomimetics made from various modified amino acids and peptide structures, such as D-amino acids and cyclopeptides.
  • The text highlights how these novel peptide designs can effectively bind metals and improve antimicrobial activity, presenting a valuable area of study in therapeutic development.

Article Abstract

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-, β-, γ-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.

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Source
http://dx.doi.org/10.1016/j.jinorgbio.2021.111386DOI Listing

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