Antimicrobial Peptides as Anticancer Agents: Functional Properties and Biological Activities

Molecules. 2020 Jun 19;25(12):2850. doi: 10.3390/molecules25122850.

Abstract

Antimicrobial peptides (AMPs), or host defense peptides, are small cationic or amphipathic molecules produced by prokaryotic and eukaryotic organisms that play a key role in the innate immune defense against viruses, bacteria and fungi. AMPs have either antimicrobial or anticancer activities. Indeed, cationic AMPs are able to disrupt microbial cell membranes by interacting with negatively charged phospholipids. Moreover, several peptides are capable to trigger cytotoxicity of human cancer cells by binding to negatively charged phosphatidylserine moieties which are selectively exposed on the outer surface of cancer cell plasma membranes. In addition, some AMPs, such as LTX-315, have shown to induce release of tumor antigens and potent damage associated molecular patterns by causing alterations in the intracellular organelles of cancer cells. Given the recognized medical need of novel anticancer drugs, AMPs could represent a potential source of effective therapeutic agents, either alone or in combination with other small molecules, in oncology. In this review we summarize and describe the properties and the mode of action of AMPs as well as the strategies to increase their selectivity toward specific cancer cells.

Keywords: ACPs; AMPs; anticancer peptides; antimicrobial peptides; cancer.

Publication types

  • Review

MeSH terms

  • Anti-Bacterial Agents* / chemistry
  • Anti-Bacterial Agents* / therapeutic use
  • Antineoplastic Agents* / chemistry
  • Antineoplastic Agents* / therapeutic use
  • Humans
  • Neoplasms* / drug therapy
  • Neoplasms* / immunology
  • Neoplasms* / metabolism
  • Neoplasms* / pathology
  • Oligopeptides* / chemistry
  • Oligopeptides* / therapeutic use
  • Pore Forming Cytotoxic Proteins* / chemistry
  • Pore Forming Cytotoxic Proteins* / therapeutic use

Substances

  • Anti-Bacterial Agents
  • Antineoplastic Agents
  • LTX-315
  • Oligopeptides
  • Pore Forming Cytotoxic Proteins