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

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.

First Report of Ocellatin-VT from the Skin Secretion of Leptodactylus vastus Lutz (Amphibia: Leptodactylidae)

“…The secretion released through the integument of anurans, mainly by the granular glands, is rich in bioactive peptides and has been the subject of different studies, especially on antimicrobial peptides (AMPs), which act on different targets such as fungi, bacteria, and viruses [7][8][9]. Ocellatins are AMPs found in the secretion of leptodactylid anurans [10].…”