Antimicrobial and antitumor properties of anuran peptide temporin-SHf induce apoptosis in A549 lung cancer cells

Amino Acids. 2024 Feb 6;56(1):12. doi: 10.1007/s00726-023-03373-3.

Abstract

Temporin-SHf is a linear, ultra-short, hydrophobic, α-helix, and phe-rich cationic antimicrobial peptide. The antitumor activities and mechanism of temporin-SHf-induced cancer cell death are unknown. The temporin-SHf was synthesized by solid-phase Fmoc chemistry and antimicrobial and antitumor activities were investigated. Temporin-SHf was microbiocidal, non-hemolytic, and cytotoxic to human cancer cells but not to non-tumorigenic cells. It affected the cancer cells' lysosomal integrity and caused cell membrane damage. The temporin-SHf inhibited A549 cancer cell proliferation and migration. It is anti-angiogenic and causes cancer cell death through apoptosis. The molecular mechanism of action of temporin-SHf confirmed that it kills cancer cells by triggering caspase-dependent apoptosis through an intrinsic mitochondrial pathway. Owing to its short length and broad spectrum of antitumor activity, temporin-SHf is a promising candidate for developing a new class of anticancer drugs.

Keywords: A549 cells; Angiogenesis; Anticancer peptides; Apoptosis; Cytotoxicity; Temporin-SHf.

MeSH terms

  • Animals
  • Anti-Infective Agents*
  • Antimicrobial Cationic Peptides / pharmacology
  • Anura
  • Apoptosis
  • Humans
  • Lung Neoplasms* / drug therapy

Substances

  • temporin
  • Antimicrobial Cationic Peptides
  • Anti-Infective Agents