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

J Inorg Biochem. 2021 Apr:217:111386. doi: 10.1016/j.jinorgbio.2021.111386. Epub 2021 Feb 10.

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.

Keywords: Antimicrobial peptides; Metal binding sites; Peptidomimetics.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acids / chemistry*
  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / pharmacology
  • Bacteria / drug effects
  • Binding Sites
  • Chelating Agents / chemistry*
  • Chelating Agents / pharmacology
  • Humans
  • Peptides, Cyclic / chemistry*
  • Peptides, Cyclic / pharmacology
  • Peptidomimetics / chemistry*
  • Peptidomimetics / pharmacology
  • Peptoids / chemistry*
  • Peptoids / pharmacology
  • Stereoisomerism

Substances

  • Amino Acids
  • Anti-Bacterial Agents
  • Chelating Agents
  • Peptides, Cyclic
  • Peptidomimetics
  • Peptoids