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

Joanna Wątły, Adriana Miller, Henryk Kozłowski, Magdalena Rowińska-Żyrek

Journal: Journal of inorganic biochemistry 2022;217():111386

PMID: 33610030

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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.

Address: Faculty of Chemistry, University of Wroclaw, Joliot - Curie 14, Wroclaw 50-383, Poland. Electronic address: [email protected].; Faculty of Chemistry, University of Wroclaw, Joliot - Curie 14, Wroclaw 50-383, Poland.; Faculty of Chemistry, University of Wroclaw, Joliot - Curie 14, Wroclaw 50-383, Poland; Department of Health Sciences, University of Opole, Katowicka 68, Opole 45-060, Poland.; Faculty of Chemistry, University of Wroclaw, Joliot - Curie 14, Wroclaw 50-383, Poland. Electronic address: [email protected].

DOI: 10.1016/j.jinorgbio.2021.111386

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MeSH Terms: Amino Acids, Anti-Bacterial Agents, Bacteria, Binding Sites, Chelating Agents, Humans, Peptides, Cyclic, Peptidomimetics, Peptoids, Stereoisomerism