A Therapeutic Potential of Animal β-hairpin Antimicrobial Peptides

Curr Med Chem. 2017;24(17):1724-1746. doi: 10.2174/0929867324666170424124416.

Abstract

Endogenous antimicrobial peptides (AMPs) are evolutionary ancient molecular factors of innate immunity that play the key role in host defense. Because of the low resistance rate, AMPs have caught extensive attention as possible alternatives to conventional antibiotics. Over the last years, it has become evident that biological functions of AMPs are beyond direct killing of microbial cells. This review focuses on a relatively small family of animal host defense peptides with the β-hairpin structure stabilized by disulfide bridges. Their small size, rigid structure, stability to proteases, and plethora of biological functions, including antibacterial, antifungal, antiviral, anticancer, endotoxin-binding, metabolism- and immune- modulating activities, make natural β-hairpin AMPs an attractive molecular basis for drug design.

Keywords: Antimicrobial peptides; disulfide bridge; host defense; innate immunity; peptide therapeutics; β-hairpin structure.

Publication types

  • Review

MeSH terms

  • Animals
  • Anti-Infective Agents / chemistry*
  • Anti-Infective Agents / pharmacology
  • Antimicrobial Cationic Peptides / chemistry*
  • Antimicrobial Cationic Peptides / pharmacology
  • Antimicrobial Cationic Peptides / therapeutic use
  • Antineoplastic Agents / chemistry
  • Antineoplastic Agents / therapeutic use
  • Antineoplastic Agents / toxicity
  • Apoptosis / drug effects
  • Bacteria / drug effects
  • Drug Resistance, Bacterial / drug effects
  • Fungi / drug effects
  • Immunity, Innate
  • Neoplasms / drug therapy
  • Protein Structure, Secondary

Substances

  • Anti-Infective Agents
  • Antimicrobial Cationic Peptides
  • Antineoplastic Agents