Anticancer activities of bovine and human lactoferricin-derived peptides1

Mauricio Arias, Ashley L. Hilchie, Evan F. Haney, Jan G.M. Bolscher, M. Eric Hyndman, Robert E.W. Hancock, Hans J. Vogel

Research output: Contribution to journalArticlepeer-review

39 Citations (Scopus)

Abstract

Lactoferrin (LF) is a mammalian host defense glycoprotein with diverse biological activities. Peptides derived from the cationic region of LF possess cytotoxic activity against cancer cells in vitro and in vivo. Bovine lactoferricin (LFcinB), a peptide derived from bovine LF (bLF), exhibits broad-spectrum anticancer activity, while a similar peptide derived from human LF (hLF) is not as active. In this work, several peptides derived from the N-terminal regions of bLF and hLF were studied for their anticancer activities against leukemia and breast-cancer cells, as well as normal peripheral blood mononuclear cells. The cyclized LFcinB-CLICK peptide, which possesses a stable triazole linkage, showed improved anticancer activity, while short peptides hLF11 and bLF10 were not cytotoxic to cancer cells. Interestingly, hLF11 can act as a cell-penetrating peptide; when combined with the antimicrobial core sequence of LFcinB (RRWQWR) through either a Pro or Gly-Gly linker, toxicity to Jurkat cells increased. Together, our work extends the library of LF-derived peptides tested for anticancer activity, and identified new chimeric peptides with high cytotoxicity towards cancerous cells. Additionally, these results support the notion that short cell-penetrating peptides and antimicrobial peptides can be combined to create new adducts with increased potency.

Original languageEnglish
Pages (from-to)91-98
Number of pages8
JournalBiochemistry and Cell Biology
Volume95
Issue number1
DOIs
Publication statusPublished - 2017

Keywords

  • Anticancer
  • Breast cancer
  • Lactoferricin
  • Lactoferrin
  • Leukemia

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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